New Schiff bases with a 2,6-bis(2-aminophenylthio)pyridine moiety acting as glutathione reductase activator and inhibitors: Synthesis and molecular docking studies
  
Yazarlar (8)
Doç. Dr. Turgay TUNÇ Kırşehir Ahi Evran Üniversitesi, Türkiye
Ahmet Bugra Ortaakarsu
Gazi Üniversitesi, Türkiye
Seda Muhsir Hatipoglu
Amasya Üniversitesi, Türkiye
Serdar Karaböcek Amasya Üniversitesi, Türkiye
Nevin Karaböcek Amasya Üniversitesi, Türkiye
Necmi Dege Ondokuz Mayis University Faculty Of Science And Arts, Türkiye
Nurcan Karacan
Gazi Üniversitesi, Türkiye
Uğur Kazancı
Ondokuz Mayis University Faculty Of Science And Arts, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Journal of Molecular Structure (Q2)
Dergi ISSN 0022-2860 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili Türkçe Basım Tarihi 04-2022
Cilt / Sayı / Sayfa 1254 / 1 / – DOI 10.1016/j.molstruc.2021.132299
Makale Linki http://dx.doi.org/10.1016/j.molstruc.2021.132299
Özet
2,6-bis(2-aminophenylthio)pyridine was synthesized and identified by x-ray diffraction method. Its new Schiff bases (H2L1, H2L2, L3 and L4) were synthesized and characterized by elemental analysis, FT-IR, LC-MS, 1H NMR and 13C NMR techniques. in vitro glutathione reductase activities of the compounds were tested on yeast and human glutathione reductase. L4 enhanced both glutathione reductase activities, resulting in AC50 values of 15.06 µM and 15.89 µM, respectively. H2L1, H2L2 and L3 were found to be the inhibitors in the range of 50.09 – 55.23 µM for yeast glutathione reductase, and in the range of 56.12–66.87 µM for human glutathione reductase. According to molecular docking analysis at the xanthine binding site in human glutathione reductase (PDB: 1XAN), 2,6-bis(2-aminophenylthio)pyridine is predicted to have antimalarial property due to having a higher XP docking score than the malaria …
Anahtar Kelimeler
Glutathione reductase activator | Glutathione reductase inhibitor | Molecular docking | Schiff bases