Synthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach
Yazarlar (5)
Doç. Dr. Feyzi Sinan TOKALI Kafkas Üniversitesi, Türkiye
Doç. Dr. Parham Taslimi Bartin Üniversitesi, Türkiye
Hande Usanmaz Sinop Üniversitesi, Türkiye
Doç. Dr. Muhammet Karaman Kilis 7 Aralık Üniversitesi, Türkiye
Kıvılcım Şendil
Kafkas Üniversitesi, Türkiye
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Journal of Molecular Structure (Q3)
Dergi ISSN 0022-2860 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 05-2021
Cilt / Sayı / Sayfa 1231 / 1 / 129666–0 DOI 10.1016/j.molstruc.2020.129666
Makale Linki http://dx.doi.org/10.1016/j.molstruc.2020.129666
UAK Araştırma Alanları
Organik Kimya
Özet
In this study, eight new Schiff base derivatives (2a-h) were synthesized and their inhibition activities against Acetylcholinesterase (AChE), Butyrylcholinesterase (BChE), α-Glucosidase and Lactoperoxidase (LPO) were investigated. Structures of the synthesized compounds were characterized using 1H and 13C nuclear magnetic resonance (NMR), infrared spectroscopy (IR), and high-resolution mass spectrometry (HRMS) spectroscopic methods. AChE was inhibited by these novel Schiff bases (2a-h) in low nanomolar levels, the Ki of which differed between 592.66 ± 57.04 and 810.78 ± 84.06 nM. Against BChE, the novel compounds demonstrated Kis varying from 358.31 ± 37.88 to 577.24 ± 59.91 nM. Also, these novel Schiff bases effectively inhibited α-glucosidase, with Ki values in the range of 1.56 ± 0.32 to 14.78 ± 2.57 nM. For LPO, Ki values were in the range of 3.96 ± 0.37 to 12.75 ± 0.06 nM. For α …
Anahtar Kelimeler
Cholinesterase | Enzyme inhibition | Molecular docking | Schiffbases | Thiosemicarbazide