dc.rights.license |
DOAJ Gold, Green Published |
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dc.date.accessioned |
2021-06-03T08:21:34Z |
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dc.date.available |
2021-06-03T08:21:34Z |
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dc.date.issued |
2020 |
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dc.identifier.issn |
1475-6366 |
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dc.identifier.uri |
www.doi.org/10.1080/14756366.2020.1746784 |
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dc.identifier.uri |
https://hdl.handle.net/20.500.12619/95368 |
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dc.description |
Bu yayın 06.11.1981 tarihli ve 17506 sayılı Resmî Gazete’de yayımlanan 2547 sayılı Yükseköğretim Kanunu’nun 4/c, 12/c, 42/c ve 42/d maddelerine dayalı 12/12/2019 tarih, 543 sayılı ve 05 numaralı Üniversite Senato Kararı ile hazırlanan Sakarya Üniversitesi Açık Bilim ve Açık Akademik Arşiv Yönergesi gereğince açık akademik arşiv sistemine açık erişim olarak yüklenmiştir. |
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dc.description.abstract |
Sulphonamides are biologically important compounds with low toxicity, many bioactivities and cost-effectiveness. Eight sulphonamide derivatives were synthesised and characterised by FT-IR, C-13 NMR, H-1 NMR, LC-MS and elemental analysis. Their inhibitory effect on AChE, and carbonic anhydrase I and II enzyme activities was investigated. Their antioxidant activity was determined using different bioanalytical assays such as radical scavenging tests with ABTS(center dot+), and DPPH center dot+ as well as metal-reducing abilities with CUPRAC, and FRAP assays. All compounds showed satisfactory enzyme inhibitory potency in nanomolar concentrations against AChE and CA isoforms with K-I values ranging from 10.14 +/- 0.03 to 100.58 +/- 1.90 nM. Amine group containing derivatives showed high metal reduction activity and about 70% ABTS radical scavenging activity. Due to their antioxidant activity and AChE inhibition, these novel compounds may be considered as leads for investigations in neurodegenerative diseases. |
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dc.description.sponsorship |
King Saud University, Riyadh, Saudi ArabiaKing Saud University [RSP-2019/1] |
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dc.language |
English |
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dc.language.iso |
İngilizce |
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dc.publisher |
TAYLOR & FRANCIS LTD |
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dc.relation.isversionof |
10.1080/14756366.2020.1746784 |
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dc.rights |
info:eu-repo/semantics/openAccess |
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dc.subject |
ANHYDRASE ISOFORMS I |
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dc.subject |
CARBONIC-ANHYDRASE |
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dc.subject |
ANTIOXIDANT ACTIVITY |
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dc.subject |
HUMAN ACETYLCHOLINESTERASE |
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dc.subject |
SELECTIVE INHIBITORS |
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dc.subject |
OXIDATIVE STRESS |
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dc.subject |
DRUG DISCOVERY |
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dc.subject |
DERIVATIVES |
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dc.subject |
VITRO |
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dc.subject |
DISEASE |
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dc.subject |
Acetylcholinesterase |
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dc.subject |
carbonic anhydrase |
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dc.subject |
synthesis |
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dc.subject |
sulphonamide |
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dc.subject |
molecular docking |
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dc.title |
Synthesis, characterisation, biological evaluation and in silico studies of sulphonamide Schiff bases |
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dc.type |
Article |
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dc.contributor.authorID |
Turkes, Cuneyt/0000-0002-2932-2789 |
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dc.contributor.authorID |
Isik, Mesut/0000-0002-4677-8104 |
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dc.contributor.authorID |
Demir, Yeliz/0000-0003-3216-1098 |
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dc.contributor.authorID |
Osman, Sameh M./0000-0003-1564-7301 |
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dc.contributor.authorID |
DURGUN, Mustafa/0000-0003-3012-7582 |
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dc.contributor.authorID |
Reis, AlessanRSS/0000-0001-8486-7469 |
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dc.contributor.authorID |
akocak, suleyman/0000-0003-4506-5265 |
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dc.contributor.authorID |
Supuran, Claudiu/0000-0003-4262-0323 |
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dc.identifier.volume |
35 |
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dc.identifier.startpage |
950 |
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dc.identifier.endpage |
962 |
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dc.relation.journal |
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY |
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dc.identifier.issue |
1 |
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dc.identifier.wos |
WOS:000523492900001 |
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dc.identifier.doi |
10.1080/14756366.2020.1746784 |
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dc.identifier.eissn |
1475-6374 |
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dc.contributor.author |
Durgun, Mustafa |
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dc.contributor.author |
Turkes, Cuneyt |
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dc.contributor.author |
Isik, Mesut |
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dc.contributor.author |
Demir, Yeliz |
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dc.contributor.author |
Sakli, Ali |
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dc.contributor.author |
Kuru, Ali |
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dc.contributor.author |
Guzel, Abdussamat |
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dc.contributor.author |
Beydemir, Sukru |
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dc.contributor.author |
Akocak, Suleyman |
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dc.contributor.author |
Osman, Sameh M. |
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dc.contributor.author |
AlOthman, Zeid |
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dc.contributor.author |
Supuran, Claudiu T. |
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dc.relation.publicationcategory |
Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı |
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dc.identifier.pmıd |
32249705 |
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