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Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives
dc.creator | Kolarević, Ana | |
dc.creator | Ilić, Budimir S. | |
dc.creator | Kocić, Gordana | |
dc.creator | Džambaski, Zdravko | |
dc.creator | Šmelcerović, Andrija | |
dc.creator | Bondžić, Bojan | |
dc.date.accessioned | 2019-07-02T13:30:31Z | |
dc.date.available | 2019-07-02T13:30:31Z | |
dc.date.issued | 2018 | |
dc.identifier.issn | 0730-2312 | |
dc.identifier.uri | https://cer.ihtm.bg.ac.rs/handle/123456789/2998 | |
dc.description.abstract | Twelve new thiazolidinones were synthesized and, together with 41 previously synthesized thiazolidinones, evaluated for inhibitory activity against deoxyribonuclease I (DNase I) in vitro. Ten compounds inhibited commercial bovine pancreatic DNase I with an IC50 below 200 μM and showed to be more potent DNase I inhibitors than crystal violet (IC50 = 365.90 ± 47.33 μM), used as a positive control. Moreover, three compounds were active against DNase I in rat liver homogenate, having an IC50 below 200 μM. (3‐Methyl‐1,4‐dioxothiazolidin‐2‐ylidene)‐N‐(2‐phenylethyl)ethanamide (41) exhibited the most potent DNase I inhibition against both commercial and rat liver DNase I with IC50 values of 115.96 ± 11.70 and 151.36 ± 15.85 μM, respectively. Site Finder and molecular docking defined the thiazolidinones interactions with the most important catalytic residues of DNase I, including the H‐acceptor interaction with residues His 134 and His 252 and/or H‐donor interaction with residues Glu 39 and Asp 168. The three most active compounds against both commercial and rat liver DNase I (31, 38, and 41) exhibited favorable physico‐chemical, pharmacokinetic, and toxicological properties. These observations could be utilized to guide the rational design and optimization of novel thiazolidinone inhibitors. Thiazolidinones as novel DNase I inhibitors could have potential therapeutic applications due to the significant involvement of DNase I in the pathophysiology of many disease conditions. | sr |
dc.language.iso | en | sr |
dc.publisher | Wiley | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172020/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172044/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/171025/RS// | sr |
dc.relation | info:eu-repo/grantAgreement/MESTD/Technological Development (TD or TR)/31060/RS// | sr |
dc.rights | restrictedAccess | sr |
dc.source | Journal of Cellular Biochemistry | sr |
dc.subject | DNase I inhibition | sr |
dc.subject | molecular docking | sr |
dc.subject | synthesis | sr |
dc.subject | thiazolidinones | sr |
dc.title | Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives | en |
dc.type | article | sr |
dc.rights.license | ARR | sr |
dcterms.abstract | Бонджић, Бојан П.; Коларевић, Aна; Илић, Будимир С.; Коцић, Гордана; Джамбаски, Здравко; Шмелцеровић, Aндрија; | |
dc.rights.holder | Wiley | sr |
dc.citation.volume | 120 | |
dc.citation.issue | 1 | |
dc.citation.spage | 264 | |
dc.citation.epage | 274 | |
dc.citation.rank | M22 | |
dc.identifier.doi | 10.1002/jcb.27339 | |
dc.identifier.scopus | 2-s2.0-85052832109 | |
dc.identifier.wos | 000450823500025 | |
dc.type.version | publishedVersion | sr |