NGHIÊN CỨU XÂY DỰNG MÔ HÌNH DOCKING VÀ MÔ PHỎNG ĐỘNG LỰC HỌC PHÂN TỬ CÁC DẪN CHẤT CHALCON CÓ HOẠT TÍNH CHỐNG OXY HÓA TRÊN ENZYM OXIDASE VAP-1

Summary
Vascular adhesion protein-1 (VAP-1) is a member of the semicarbazide – sensitive amine oxidase (SSAO) enzyme family, which is involved in the pathogenesis of multiple vascular diseases. Chalcone is a simple compound of a large group of flavonoids presented in plants and widely distributed around the world. Chalcone and its derivatives have been reported to have many therapeutic effects such as anti-inflammatory, antioxidant, anti-cancer, anti-viral… This study focuses on building a docking model to evaluate binding ability of chalcone compounds on oxidase enzyme VAP-1. The crystal structures of those enzymes were downloaded from the Protein Data Bank (pdb: 4btx). The molecular docking models of chalcone’s derivatives toward VAP-1 enzyme showed that most of the compounds are well bound and able to inhibit this oxidase enzyme. Selected substances with good docking results would conduct molecular dynamics simulation to evaluate the stability and mobility of the complexes.
Keywords: Chalcone, antioxidant, VAP-1, docking, molecular dynamics simulations.

Đầu trang

Tải