- home
- Advanced Search
- European University of Technology
- Publications
- Research software
- IT
- ES
- Flore (Florence Research Repository...
- European University of Technology
- Publications
- Research software
- IT
- ES
- Flore (Florence Research Repository...
Loading
description Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Sobati, Marjan; Abdoli, Morteza; Bonardi, Alessandro; Gratteri, Paola; Supuran, Claudiu T; Žalubovskis, Raivis;A series of hitherto unknown sulfonamide-incorporated α-aminophosphonate derivatives were synthesized through the one-pot, two-step FeCl
ACS Medicinal Chemis... arrow_drop_down ACS Medicinal Chemistry LettersArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsmedchemlett.3c00200&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 0 citations 0 popularity Average influence Average impulse Average Powered by BIP!more_vert ACS Medicinal Chemis... arrow_drop_down ACS Medicinal Chemistry LettersArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsmedchemlett.3c00200&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Ali Issa; Tiziana Ritacco; Dandan Ge; Aurelie Broussier; Giuseppe Emanuele Lio; Michele Giocondo; Sylvain Blaize; Tien Hoa Nguyen; Xuan Quyen Dinh; Christophe Couteau; Renaud Bachelot; Safi Jradi;This paper reports on a new strategy for obtaining homogeneous dispersion of grafted quantum dots (QDs) in a photopolymer matrix and their use for the integration of single-photon sources by two-photon polymerization (TPP) with nanoscale precision. The method is based on phase transfer of QDs from organic solvents to an acrylic matrix. The detailed protocol is described, and the corresponding mechanism is investigated and revealed. The phase transfer is done by ligand exchange through the introduction of mono-2-(methacryloyloxy) ethyl succinate (MES) that replaces oleic acid (OA). Infrared (IR) measurements show the replacement of OA on the QD surface by MES after ligand exchange. This allows QDs to move from the hexane phase to the pentaerythritol triacrylate (PETA) phase. The QDs that are homogeneously dispersed in the photopolymer without any clusterization do not show any significant broadening in their photoluminescence spectra even after more than 3 years. The ability of the hybrid photopolymer to create micro- and nanostructures by two-photon polymerization is demonstrated. The homogeneity of emission from 2D and 3D microstructures is confirmed by confocal photoluminescence microscopy. The fabrication and integration of a single-photon source in a spatially controlled manner by TPP is achieved and confirmed by auto-correlation measurements.
Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository); ACS Applied Materials & InterfacesArticle . 2023 . Peer-reviewedLicense: STM Policy #29add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsami.2c22533&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository); ACS Applied Materials & InterfacesArticle . 2023 . Peer-reviewedLicense: STM Policy #29add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsami.2c22533&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 Finland, ItalyPublisher:MDPI AG Morteza Abdoli; Alessandro Bonardi; Niccolò Paoletti; Ashok Aspatwar; Seppo Parkkila; Paola Gratteri; Claudiu T. Supuran; Raivis Žalubovskis;handle: 2158/1347986
A library of structurally diverse N-((4-sulfamoylphenyl)carbamothioyl) amides was synthesized by selective acylation of easily accessible 4-thioureidobenzenesulfonamide with various aliphatic, benzylic, vinylic and aromatic acyl chlorides under mild conditions. Inhibition of three α-class cytosolic human (h) carbonic anhydrases (CAs) (EC 4.2.1.1); that is, hCA I, hCA II and hCA VII and three bacterial β-CAs from Mycobacterium tuberculosis (MtCA1-MtCA3) with these sulfonamides was thereafter investigated in vitro and in silico. Many of the evaluated compounds displayed better inhibition against hCA I (KI = 13.3–87.6 nM), hCA II (KI = 5.3–384.3 nM), and hCA VII (KI = 1.1–13.5 nM) compared with acetazolamide (AAZ) as the control drug (KI values of 250, 12.5 and 2.5 nM, respectively, against hCA I, hCA II and hCA VII). The mycobacterial enzymes MtCA1 and MtCA2 were also effectively inhibited by these compounds. MtCA3 was, on the other hand, poorly inhibited by the sulfonamides reported here. The most sensitive mycobacterial enzyme to these inhibitors was MtCA2 in which 10 of the 12 evaluated compounds showed KIs (KI, the inhibitor constant) in the low nanomolar range.
Molecules arrow_drop_down MoleculesOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYFull-Text: http://www.mdpi.com/1420-3049/28/10/4020/pdfTrepo - Institutional Repository of Tampere UniversityArticle . 2023 . Peer-reviewedData sources: Trepo - Institutional Repository of Tampere UniversityFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.3390/molecules28104020&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 2 citations 2 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Molecules arrow_drop_down MoleculesOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYFull-Text: http://www.mdpi.com/1420-3049/28/10/4020/pdfTrepo - Institutional Repository of Tampere UniversityArticle . 2023 . Peer-reviewedData sources: Trepo - Institutional Repository of Tampere UniversityFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.3390/molecules28104020&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Jekateri̅na Ivanova; Alessio Nocentini; Kaspars Ta̅rs; Ja̅nis Leita̅ns; Elviss Dvinskis; Andris Kazaks; Ilona Domračeva; Claudiu T. Supuran; Raivis Žalubovskis;Here, we report for the first time a series of sulfonamide derivatives with scaffolds bearing flexible moieties, namely, rotamers or tropoisomers capable of adapting their geometry in the active center of enzymes thus being effective and selective carbonic anhydrase (CAs, EC 4.2.1.1) enzyme inhibitors. All compounds exhibited effective in vitro inhibition activity toward the main hCA isoforms related to cancer (i.e., hCA II, hCA IX, and hCA XII with
Journal of Medicinal... arrow_drop_down Journal of Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acs.jmedchem.3c00007&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 2 citations 2 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Journal of Medicinal... arrow_drop_down Journal of Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acs.jmedchem.3c00007&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Authors: Morteza Abdoli; Claudiu T. Supuran; Raivis Žalubovskis;Morteza Abdoli; Claudiu T. Supuran; Raivis Žalubovskis;AbstractA small library of substituted cyclic guanidine incorporated benzothiazole-6-sulphonamides was synthesized. All obtained compounds were investigated for their inhibitory activity against the key brain-associated human carbonic anhydrase isoform hCA VII (a promising target for the treatment of neuropathic pain) and three isoforms expressed in brain and other tissues, hCA I, II, and IV. Sulphaguanidine derivatives 9a–d were inactive on the all investigated isoforms while the primary sulphonamide containing guanidines 6a–c and 7a–c were inactive towards hCA IV but displayed inhibiting properties on hCA I, II, and VII with KIs values in the low nanomolar to micromolar ranges. The results indicated that isoforms hCA II and VII were potently and selectively inhibited by these compounds, whereas the cytosolic hCA I was less sensitive to inhibition. The derivatives reported in this study might be useful for design of more potent and selective inhibitors of hCA II and VII.
Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2174981&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 6 citations 6 popularity Top 10% influence Average impulse Top 10% Powered by BIP!more_vert Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2174981&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Wiley Morteza, Abdoli; Viviana, De Luca; Clemente, Capasso; Claudiu T, Supuran; Raivis, Žalubovskis;AbstractTwo novel sulfaguanidine series, six N‐(N,N′‐dialkyl/dibenzyl‐carbamimidoyl) benzenesulfonamide derivatives and nine N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamide derivatives, were obtained by desulfidative amination of easily accessible dimethyl arylsulfonylcarbonimidodithioates under catalyst‐ and base‐free conditions. The newly synthesized compounds were tested for the inhibition of four different isozymes of human carbonic anhydrase (hCA I, II, IX and XII, EC 4.2.1.1). Both series reported here were inactive against the off‐target isozymes hCA I and II (Ki>100 μM). Interestingly, all investigated compounds inhibited both target isozymes hCA IX and XII in the submicromolar to micromolar ranges in which Ki values spanned from 0.168 to 0.921 μM against hCA IX and from 0.335 to 1.451 μM against hCA XII. The results indicated that N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamides were slightly more potent inhibitors than N‐(N,N′‐dialkyl/dibenzyl‐carbamimidoyl) benzenesulfonamides. Among the evaluated compounds, N‐n‐octyl‐substituted N‐carbamimidoylbenzenesulfonamide showed the most significant activity with a Ki value of 0.168 μM against hCA IX, which was four‐fold more selective toward this isozyme versus hCA XII. Again, another derivative from N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamide series, N‐p‐methylbenzyl‐substituted N‐carbamimidoylbenzenesulfonamide, demonstrated superior inhibitory activity against hCA XII with a Ki value of 0.335 μM.
Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)ChemMedChemArticle . 2023 . Peer-reviewedLicense: Wiley Online Library User AgreementData sources: Crossrefadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1002/cmdc.202200658&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)ChemMedChemArticle . 2023 . Peer-reviewedLicense: Wiley Online Library User AgreementData sources: Crossrefadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1002/cmdc.202200658&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Jekaterīna Ivanova; Morteza Abdoli; Alessio Nocentini; Raivis Žalubovskis; Claudiu T. Supuran;AbstractA series of 4-methyl-1,2,3-benzoxathiazine-2,2-dioxides with various substituents in 5, 6 or 7 positions was obtained from corresponding 2’-hydroxyacetophenones in their reaction with sulphamoyl chloride. 6- and 7-aryl substituted 4-methyl-1,2,3-benzoxathiazine-2,2-dioxides were obtained from aryl substituted 2’-hydroxyacetophenonesprepared from 4- or 5-bromo-2’-hydroxyacetophenones via two-step protocol. 4-Methyl-1,2,3-benzoxathiazine-2,2-dioxides were investigated as inhibitors of four human (h) carbonic anhydrase (hCA, EC 4.2.1.1) isoforms, off-target cytosolic hCA I and II, and target transmembrane, tumour-associated hCA IX and XII. Twenty derivatives of 4-methyl-1,2,3-benzoxathiazine 2,2-dioxide were obtained. With one exception (compound2a), they mostly act as nanomolar inhibitors of target hCA IX and XII. Basically, all screened compounds express none or low inhibitory properties towards off-target hCA I. hCA II is inhibited in micromolar range. Overwhelming majority of 4-methyl-1,2,3-benzoxathiazine 2,2-dioxides express excellent selectivity towards CA IX/XII over hCA I as well as very good selectivity towards CA IX/XII over hCA II.
Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2170370&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 6 citations 6 popularity Top 10% influence Average impulse Top 10% Powered by BIP!more_vert Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2170370&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 Belgium, Italy, DenmarkPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDPlotniece, Aiva; Sobolev, Arkadij; Supuran, Claudiu T.; Carta, Fabrizio; Björkling, Fredrik; Franzyk, Henrik; Yli-Kauhaluoma, Jari; Augustyns, Koen; Cos, Paul; De Vooght, Linda; Govaerts, Matthias; Aizawa, Juliana; Tammela, Päivi; Žalubovskis, Raivis;Abstract: Natural products and analogues are a source of antibacterial drug discovery. Considering drug resistance levels emerging for antibiotics, identification of bacterial metalloenzymes and the synthesis of selective inhibitors are interesting for antibacterial agent development. Peptide nucleic acids are attractive antisense and antigene agents representing a novel strategy to target pathogens due to their unique mechanism of action. Antisense inhibition and development of antisense peptide nucleic acids is a new approach to antibacterial agents. Due to the increased resistance of biofilms to antibiotics, alternative therapeutic options are necessary. To develop antimicrobial strategies, optimised in vitro and in vivo models are needed. In vivo models to study biofilm-related respiratory infections, device-related infections: ventilator-associated pneumonia, tissue-related infections: chronic infection models based on alginate or agar beads, methods to battle biofilm-related infections are discussed. Drug delivery in case of antibacterials often is a serious issue therefore this review includes overview of drug delivery nanosystems
ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Institutional Repository Universiteit AntwerpenCopenhagen University Research Information SystemArticle . 2023Data sources: Copenhagen University Research Information SystemJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2155816&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 15 citations 15 popularity Top 10% influence Average impulse Top 10% Powered by BIP!visibility 8visibility views 8 download downloads 20 Powered bymore_vert ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Institutional Repository Universiteit AntwerpenCopenhagen University Research Information SystemArticle . 2023Data sources: Copenhagen University Research Information SystemJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2155816&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDAuthors: Abdoli, Morteza; Bonardi, Alessandro; Supuran, Claudiu T.; Žalubovskis, Raivis;Abdoli, Morteza; Bonardi, Alessandro; Supuran, Claudiu T.; Žalubovskis, Raivis;AbstractA library of novel alkyl/benzyl (4-sulphamoylphenyl)carbamimidothioates was synthesised by selective S-alkylation of the easily accessible 4-thioureidobenzenesulphonamide. The compounds were assayed as inhibitors of four human (h) carbonic anhydrase isoforms hCA I, II, VII, and XIII, as well as three bacterial enzymes belonging to the β-CA class, MscCA from Mammaliicoccus (Staphylococcus) sciuri and StCA1 and StCA2, from Salmonella enterica (serovar Typhimurium). Most compounds investigated here exhibited moderate to low nanomolar inhibition constants against hCA I, II, and VII. The cytosolic hCA XIII was also inhibited by these compounds, but not as effective as hCA I, II, and VII. Several compounds were very effective against MscCA and StCA1. StCA2 was less inhibited compared to MscCA and StCA1. Some compounds showed considerable selectivity for inhibiting some CA isoforms. They may thus be considered as interesting starting points for the discovery and development of novel therapeutic agents belonging to this class of enzyme inhibitors.
ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2152811&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 5 citations 5 popularity Top 10% influence Average impulse Average Powered by BIP!visibility 11visibility views 11 download downloads 12 Powered bymore_vert ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2152811&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDAbdoli, Morteza; De Luca, Viviana; Capasso, Clemente; Supuran, Claudiu T.; Žalubovskis, Raivis;A small library of novel thiazolone-benzenesulphonamides has been prepared and evaluated for their ability to inhibit three human cytosolic carbonic anhydrases (hCA I, hCA II, and hCA VII) and three bacterial carbonic anhydrases (MscCA beta, StCA1, and StCA2). All investigated hCAs were inhibited by the prepared compounds 4a-4j in the low nanomolar range. These compounds were effective hCA I inhibitors (K(I)s of 31.5-637.3 nM) and excellent hCA II (K(I)s in the range of 1.3-13.7 nM) and hCA VII inhibitors (K(I)s in the range of 0.9-14.6 nM). The most active analog in the series, 4-((4-oxo-5-propyl-4,5-dihydrothiazol-2-yl)amino)benzenesulphonamide 4d, strongly inhibited bacterial MscCA beta, with K-I of 73.6 nM, considerably better than AAZ (K-I of 625 nM). The tested compounds displayed medium inhibitory potency against StCA1 (K(I)s of 69.2-163.3 nM) when compared to the standard drug (K-I of 59 nM). However, StCA2 was poorly inhibited by the sulphonamides reported here, with K(I)s in the micromolar range between 275.2 and 4875.0 nM.
ZENODO; Journal of E... arrow_drop_down ZENODO; Journal of Enzyme Inhibition and Medicinal ChemistryOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2163243&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!visibility 7visibility views 7 download downloads 9 Powered bymore_vert ZENODO; Journal of E... arrow_drop_down ZENODO; Journal of Enzyme Inhibition and Medicinal ChemistryOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2163243&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu
Loading
description Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Sobati, Marjan; Abdoli, Morteza; Bonardi, Alessandro; Gratteri, Paola; Supuran, Claudiu T; Žalubovskis, Raivis;A series of hitherto unknown sulfonamide-incorporated α-aminophosphonate derivatives were synthesized through the one-pot, two-step FeCl
ACS Medicinal Chemis... arrow_drop_down ACS Medicinal Chemistry LettersArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsmedchemlett.3c00200&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 0 citations 0 popularity Average influence Average impulse Average Powered by BIP!more_vert ACS Medicinal Chemis... arrow_drop_down ACS Medicinal Chemistry LettersArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsmedchemlett.3c00200&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Ali Issa; Tiziana Ritacco; Dandan Ge; Aurelie Broussier; Giuseppe Emanuele Lio; Michele Giocondo; Sylvain Blaize; Tien Hoa Nguyen; Xuan Quyen Dinh; Christophe Couteau; Renaud Bachelot; Safi Jradi;This paper reports on a new strategy for obtaining homogeneous dispersion of grafted quantum dots (QDs) in a photopolymer matrix and their use for the integration of single-photon sources by two-photon polymerization (TPP) with nanoscale precision. The method is based on phase transfer of QDs from organic solvents to an acrylic matrix. The detailed protocol is described, and the corresponding mechanism is investigated and revealed. The phase transfer is done by ligand exchange through the introduction of mono-2-(methacryloyloxy) ethyl succinate (MES) that replaces oleic acid (OA). Infrared (IR) measurements show the replacement of OA on the QD surface by MES after ligand exchange. This allows QDs to move from the hexane phase to the pentaerythritol triacrylate (PETA) phase. The QDs that are homogeneously dispersed in the photopolymer without any clusterization do not show any significant broadening in their photoluminescence spectra even after more than 3 years. The ability of the hybrid photopolymer to create micro- and nanostructures by two-photon polymerization is demonstrated. The homogeneity of emission from 2D and 3D microstructures is confirmed by confocal photoluminescence microscopy. The fabrication and integration of a single-photon source in a spatially controlled manner by TPP is achieved and confirmed by auto-correlation measurements.
Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository); ACS Applied Materials & InterfacesArticle . 2023 . Peer-reviewedLicense: STM Policy #29add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsami.2c22533&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository); ACS Applied Materials & InterfacesArticle . 2023 . Peer-reviewedLicense: STM Policy #29add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acsami.2c22533&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 Finland, ItalyPublisher:MDPI AG Morteza Abdoli; Alessandro Bonardi; Niccolò Paoletti; Ashok Aspatwar; Seppo Parkkila; Paola Gratteri; Claudiu T. Supuran; Raivis Žalubovskis;handle: 2158/1347986
A library of structurally diverse N-((4-sulfamoylphenyl)carbamothioyl) amides was synthesized by selective acylation of easily accessible 4-thioureidobenzenesulfonamide with various aliphatic, benzylic, vinylic and aromatic acyl chlorides under mild conditions. Inhibition of three α-class cytosolic human (h) carbonic anhydrases (CAs) (EC 4.2.1.1); that is, hCA I, hCA II and hCA VII and three bacterial β-CAs from Mycobacterium tuberculosis (MtCA1-MtCA3) with these sulfonamides was thereafter investigated in vitro and in silico. Many of the evaluated compounds displayed better inhibition against hCA I (KI = 13.3–87.6 nM), hCA II (KI = 5.3–384.3 nM), and hCA VII (KI = 1.1–13.5 nM) compared with acetazolamide (AAZ) as the control drug (KI values of 250, 12.5 and 2.5 nM, respectively, against hCA I, hCA II and hCA VII). The mycobacterial enzymes MtCA1 and MtCA2 were also effectively inhibited by these compounds. MtCA3 was, on the other hand, poorly inhibited by the sulfonamides reported here. The most sensitive mycobacterial enzyme to these inhibitors was MtCA2 in which 10 of the 12 evaluated compounds showed KIs (KI, the inhibitor constant) in the low nanomolar range.
Molecules arrow_drop_down MoleculesOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYFull-Text: http://www.mdpi.com/1420-3049/28/10/4020/pdfTrepo - Institutional Repository of Tampere UniversityArticle . 2023 . Peer-reviewedData sources: Trepo - Institutional Repository of Tampere UniversityFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.3390/molecules28104020&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 2 citations 2 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Molecules arrow_drop_down MoleculesOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYFull-Text: http://www.mdpi.com/1420-3049/28/10/4020/pdfTrepo - Institutional Repository of Tampere UniversityArticle . 2023 . Peer-reviewedData sources: Trepo - Institutional Repository of Tampere UniversityFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.3390/molecules28104020&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:American Chemical Society (ACS) Jekateri̅na Ivanova; Alessio Nocentini; Kaspars Ta̅rs; Ja̅nis Leita̅ns; Elviss Dvinskis; Andris Kazaks; Ilona Domračeva; Claudiu T. Supuran; Raivis Žalubovskis;Here, we report for the first time a series of sulfonamide derivatives with scaffolds bearing flexible moieties, namely, rotamers or tropoisomers capable of adapting their geometry in the active center of enzymes thus being effective and selective carbonic anhydrase (CAs, EC 4.2.1.1) enzyme inhibitors. All compounds exhibited effective in vitro inhibition activity toward the main hCA isoforms related to cancer (i.e., hCA II, hCA IX, and hCA XII with
Journal of Medicinal... arrow_drop_down Journal of Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acs.jmedchem.3c00007&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 2 citations 2 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Journal of Medicinal... arrow_drop_down Journal of Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: STM Policy #29Data sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1021/acs.jmedchem.3c00007&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Authors: Morteza Abdoli; Claudiu T. Supuran; Raivis Žalubovskis;Morteza Abdoli; Claudiu T. Supuran; Raivis Žalubovskis;AbstractA small library of substituted cyclic guanidine incorporated benzothiazole-6-sulphonamides was synthesized. All obtained compounds were investigated for their inhibitory activity against the key brain-associated human carbonic anhydrase isoform hCA VII (a promising target for the treatment of neuropathic pain) and three isoforms expressed in brain and other tissues, hCA I, II, and IV. Sulphaguanidine derivatives 9a–d were inactive on the all investigated isoforms while the primary sulphonamide containing guanidines 6a–c and 7a–c were inactive towards hCA IV but displayed inhibiting properties on hCA I, II, and VII with KIs values in the low nanomolar to micromolar ranges. The results indicated that isoforms hCA II and VII were potently and selectively inhibited by these compounds, whereas the cytosolic hCA I was less sensitive to inhibition. The derivatives reported in this study might be useful for design of more potent and selective inhibitors of hCA II and VII.
Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2174981&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 6 citations 6 popularity Top 10% influence Average impulse Top 10% Powered by BIP!more_vert Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2174981&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Wiley Morteza, Abdoli; Viviana, De Luca; Clemente, Capasso; Claudiu T, Supuran; Raivis, Žalubovskis;AbstractTwo novel sulfaguanidine series, six N‐(N,N′‐dialkyl/dibenzyl‐carbamimidoyl) benzenesulfonamide derivatives and nine N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamide derivatives, were obtained by desulfidative amination of easily accessible dimethyl arylsulfonylcarbonimidodithioates under catalyst‐ and base‐free conditions. The newly synthesized compounds were tested for the inhibition of four different isozymes of human carbonic anhydrase (hCA I, II, IX and XII, EC 4.2.1.1). Both series reported here were inactive against the off‐target isozymes hCA I and II (Ki>100 μM). Interestingly, all investigated compounds inhibited both target isozymes hCA IX and XII in the submicromolar to micromolar ranges in which Ki values spanned from 0.168 to 0.921 μM against hCA IX and from 0.335 to 1.451 μM against hCA XII. The results indicated that N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamides were slightly more potent inhibitors than N‐(N,N′‐dialkyl/dibenzyl‐carbamimidoyl) benzenesulfonamides. Among the evaluated compounds, N‐n‐octyl‐substituted N‐carbamimidoylbenzenesulfonamide showed the most significant activity with a Ki value of 0.168 μM against hCA IX, which was four‐fold more selective toward this isozyme versus hCA XII. Again, another derivative from N‐(N‐alkyl/benzyl‐carbamimidoyl) benzenesulfonamide series, N‐p‐methylbenzyl‐substituted N‐carbamimidoylbenzenesulfonamide, demonstrated superior inhibitory activity against hCA XII with a Ki value of 0.335 μM.
Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)ChemMedChemArticle . 2023 . Peer-reviewedLicense: Wiley Online Library User AgreementData sources: Crossrefadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1002/cmdc.202200658&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesbronze 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!more_vert Flore (Florence Rese... arrow_drop_down Flore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)ChemMedChemArticle . 2023 . Peer-reviewedLicense: Wiley Online Library User AgreementData sources: Crossrefadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1002/cmdc.202200658&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Jekaterīna Ivanova; Morteza Abdoli; Alessio Nocentini; Raivis Žalubovskis; Claudiu T. Supuran;AbstractA series of 4-methyl-1,2,3-benzoxathiazine-2,2-dioxides with various substituents in 5, 6 or 7 positions was obtained from corresponding 2’-hydroxyacetophenones in their reaction with sulphamoyl chloride. 6- and 7-aryl substituted 4-methyl-1,2,3-benzoxathiazine-2,2-dioxides were obtained from aryl substituted 2’-hydroxyacetophenonesprepared from 4- or 5-bromo-2’-hydroxyacetophenones via two-step protocol. 4-Methyl-1,2,3-benzoxathiazine-2,2-dioxides were investigated as inhibitors of four human (h) carbonic anhydrase (hCA, EC 4.2.1.1) isoforms, off-target cytosolic hCA I and II, and target transmembrane, tumour-associated hCA IX and XII. Twenty derivatives of 4-methyl-1,2,3-benzoxathiazine 2,2-dioxide were obtained. With one exception (compound2a), they mostly act as nanomolar inhibitors of target hCA IX and XII. Basically, all screened compounds express none or low inhibitory properties towards off-target hCA I. hCA II is inhibited in micromolar range. Overwhelming majority of 4-methyl-1,2,3-benzoxathiazine 2,2-dioxides express excellent selectivity towards CA IX/XII over hCA I as well as very good selectivity towards CA IX/XII over hCA II.
Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2170370&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 6 citations 6 popularity Top 10% influence Average impulse Top 10% Powered by BIP!more_vert Journal of Enzyme In... arrow_drop_down Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2023.2170370&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 Belgium, Italy, DenmarkPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDPlotniece, Aiva; Sobolev, Arkadij; Supuran, Claudiu T.; Carta, Fabrizio; Björkling, Fredrik; Franzyk, Henrik; Yli-Kauhaluoma, Jari; Augustyns, Koen; Cos, Paul; De Vooght, Linda; Govaerts, Matthias; Aizawa, Juliana; Tammela, Päivi; Žalubovskis, Raivis;Abstract: Natural products and analogues are a source of antibacterial drug discovery. Considering drug resistance levels emerging for antibiotics, identification of bacterial metalloenzymes and the synthesis of selective inhibitors are interesting for antibacterial agent development. Peptide nucleic acids are attractive antisense and antigene agents representing a novel strategy to target pathogens due to their unique mechanism of action. Antisense inhibition and development of antisense peptide nucleic acids is a new approach to antibacterial agents. Due to the increased resistance of biofilms to antibiotics, alternative therapeutic options are necessary. To develop antimicrobial strategies, optimised in vitro and in vivo models are needed. In vivo models to study biofilm-related respiratory infections, device-related infections: ventilator-associated pneumonia, tissue-related infections: chronic infection models based on alginate or agar beads, methods to battle biofilm-related infections are discussed. Drug delivery in case of antibacterials often is a serious issue therefore this review includes overview of drug delivery nanosystems
ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Institutional Repository Universiteit AntwerpenCopenhagen University Research Information SystemArticle . 2023Data sources: Copenhagen University Research Information SystemJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2155816&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 15 citations 15 popularity Top 10% influence Average impulse Top 10% Powered by BIP!visibility 8visibility views 8 download downloads 20 Powered bymore_vert ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Institutional Repository Universiteit AntwerpenCopenhagen University Research Information SystemArticle . 2023Data sources: Copenhagen University Research Information SystemJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2155816&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDAuthors: Abdoli, Morteza; Bonardi, Alessandro; Supuran, Claudiu T.; Žalubovskis, Raivis;Abdoli, Morteza; Bonardi, Alessandro; Supuran, Claudiu T.; Žalubovskis, Raivis;AbstractA library of novel alkyl/benzyl (4-sulphamoylphenyl)carbamimidothioates was synthesised by selective S-alkylation of the easily accessible 4-thioureidobenzenesulphonamide. The compounds were assayed as inhibitors of four human (h) carbonic anhydrase isoforms hCA I, II, VII, and XIII, as well as three bacterial enzymes belonging to the β-CA class, MscCA from Mammaliicoccus (Staphylococcus) sciuri and StCA1 and StCA2, from Salmonella enterica (serovar Typhimurium). Most compounds investigated here exhibited moderate to low nanomolar inhibition constants against hCA I, II, and VII. The cytosolic hCA XIII was also inhibited by these compounds, but not as effective as hCA I, II, and VII. Several compounds were very effective against MscCA and StCA1. StCA2 was less inhibited compared to MscCA and StCA1. Some compounds showed considerable selectivity for inhibiting some CA isoforms. They may thus be considered as interesting starting points for the discovery and development of novel therapeutic agents belonging to this class of enzyme inhibitors.
ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2152811&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 5 citations 5 popularity Top 10% influence Average impulse Average Powered by BIP!visibility 11visibility views 11 download downloads 12 Powered bymore_vert ZENODO; Flore (Flore... arrow_drop_down ZENODO; Flore (Florence Research Repository); Journal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2152811&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article 2023 ItalyPublisher:Informa UK Limited Funded by:EC | SPRINGBOARDEC| SPRINGBOARDAbdoli, Morteza; De Luca, Viviana; Capasso, Clemente; Supuran, Claudiu T.; Žalubovskis, Raivis;A small library of novel thiazolone-benzenesulphonamides has been prepared and evaluated for their ability to inhibit three human cytosolic carbonic anhydrases (hCA I, hCA II, and hCA VII) and three bacterial carbonic anhydrases (MscCA beta, StCA1, and StCA2). All investigated hCAs were inhibited by the prepared compounds 4a-4j in the low nanomolar range. These compounds were effective hCA I inhibitors (K(I)s of 31.5-637.3 nM) and excellent hCA II (K(I)s in the range of 1.3-13.7 nM) and hCA VII inhibitors (K(I)s in the range of 0.9-14.6 nM). The most active analog in the series, 4-((4-oxo-5-propyl-4,5-dihydrothiazol-2-yl)amino)benzenesulphonamide 4d, strongly inhibited bacterial MscCA beta, with K-I of 73.6 nM, considerably better than AAZ (K-I of 625 nM). The tested compounds displayed medium inhibitory potency against StCA1 (K(I)s of 69.2-163.3 nM) when compared to the standard drug (K-I of 59 nM). However, StCA2 was poorly inhibited by the sulphonamides reported here, with K(I)s in the micromolar range between 275.2 and 4875.0 nM.
ZENODO; Journal of E... arrow_drop_down ZENODO; Journal of Enzyme Inhibition and Medicinal ChemistryOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2163243&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess Routesgold 4 citations 4 popularity Top 10% influence Average impulse Average Powered by BIP!visibility 7visibility views 7 download downloads 9 Powered bymore_vert ZENODO; Journal of E... arrow_drop_down ZENODO; Journal of Enzyme Inhibition and Medicinal ChemistryOther literature type . Article . 2023 . Peer-reviewedLicense: CC BYJournal of Enzyme Inhibition and Medicinal ChemistryArticle . 2023Data sources: Europe PubMed CentralFlore (Florence Research Repository)Article . 2023Data sources: Flore (Florence Research Repository)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1080/14756366.2022.2163243&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu