Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives
Samo za registrovane korisnike
2018
Autori
Kolarević, AnaIlić, Budimir S.
Kocić, Gordana
Džambaski, Zdravko
Šmelcerović, Andrija
Bondžić, Bojan
Članak u časopisu (Objavljena verzija)
,
Wiley
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
DNase I inhibition / molecular docking / synthesis / thiazolidinonesIzvor:
Journal of Cellular Biochemistry, 2018, 120, 1, 264-274Izdavač:
- Wiley
Finansiranje / projekti:
- Eksperimentalna i teorijska proučavanja reaktivnosti i biološka aktivnost stereodefinisanih tiazolidina i sintetičkih analoga (RS-172020)
- Dobijanje, fizičko-hemijska karakterizacija, analitika i biološka aktivnost farmakološki aktivnih supstanci (RS-172044)
- Električni proboj gasova, površinski procesi i primene (RS-171025)
- Proizvodnja novih dijetetskih mlečnih proizvoda za rizične populacije zasnovana na kvalitativnoj i kvantitativnoj analizi biohemijskih markera zdravstvenog rizika konzumiranja mleka (RS-31060)
DOI: 10.1002/jcb.27339
ISSN: 0730-2312
WoS: 000450823500025
Scopus: 2-s2.0-85052832109
Institucija/grupa
IHTMTY - JOUR AU - Kolarević, Ana AU - Ilić, Budimir S. AU - Kocić, Gordana AU - Džambaski, Zdravko AU - Šmelcerović, Andrija AU - Bondžić, Bojan PY - 2018 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2998 AB - 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. PB - Wiley T2 - Journal of Cellular Biochemistry T1 - Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives VL - 120 IS - 1 SP - 264 EP - 274 DO - 10.1002/jcb.27339 ER -
@article{ author = "Kolarević, Ana and Ilić, Budimir S. and Kocić, Gordana and Džambaski, Zdravko and Šmelcerović, Andrija and Bondžić, Bojan", year = "2018", 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.", publisher = "Wiley", journal = "Journal of Cellular Biochemistry", title = "Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives", volume = "120", number = "1", pages = "264-274", doi = "10.1002/jcb.27339" }
Kolarević, A., Ilić, B. S., Kocić, G., Džambaski, Z., Šmelcerović, A.,& Bondžić, B.. (2018). Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives. in Journal of Cellular Biochemistry Wiley., 120(1), 264-274. https://doi.org/10.1002/jcb.27339
Kolarević A, Ilić BS, Kocić G, Džambaski Z, Šmelcerović A, Bondžić B. Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives. in Journal of Cellular Biochemistry. 2018;120(1):264-274. doi:10.1002/jcb.27339 .
Kolarević, Ana, Ilić, Budimir S., Kocić, Gordana, Džambaski, Zdravko, Šmelcerović, Andrija, Bondžić, Bojan, "Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives" in Journal of Cellular Biochemistry, 120, no. 1 (2018):264-274, https://doi.org/10.1002/jcb.27339 . .