Synthesis, characterization, biological activity and molecular docking studies of novel schiff bases derived from thiosemicarbazide: Biochemical and computational approach
Yazarlar (5)
Kıvılcım Şendil Kafkas Üniversitesi, Türkiye
Feyzi Sinan Tokalı Kafkas Üniversitesi, Türkiye
Muhammet Karaman Kilis 7 Aralık Üniversitesi, Türkiye
Dr. Öğr. Üyesi Hande USANMAZ Sinop Üniversitesi, Türkiye
Parham Taslimi
Makale Türü Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı JOURNAL OF MOLECULAR STRUCTURE (Q3)
Dergi ISSN 0022-2860 Dergi Bilgileri (2021)
Dergi Tarandığı Indeksler SCI-Expanded
Makale Dili İngilizce Basım Tarihi 05-2021
Kabul Tarihi Yayınlanma Tarihi 01-05-2021
Cilt / Sayı / Sayfa 1231 / 0 / 129666–0 DOI 10.1016/j.molstruc.2020.129666
Makale Linki http://dx.doi.org/10.1016/j.molstruc.2020.129666
UAK Araştırma Alanları
Biyokimya
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
Schiffbases | Thiosemicarbazide | Cholinesterase | Enzyme inhibition | Molecular docking