Molecular Docking and Reaction Kinetic Studies of Chrysin Binding to Serum Albumin-Reference-Cited by-同舟云学术

Molecular Docking and Reaction Kinetic Studies of Chrysin Binding to Serum Albumin

Published:2014-02 Issue:2 Volume:9 Page:1934578X1400900
ISSN:1934-578X
Container-title:Natural Product Communications
language:en
Short-container-title:Natural Product Communications

Author:

Jiang Bingli¹,Zhao Anran²,Miao Jianhua³,Chang Pengfei¹,Chen Hailin¹,Pan Weigao¹³,Lin Cuiwu¹

Affiliation:

1. School of Chemistry and Chemical Engineering, Guangxi University, Nanning, Guangxi, 530004 P. R. China

2. Department of Chemistry, College of Sciences and Health Professions, Cleveland State University, Cleveland OH 44115, USA

3. Guangxi Botanical Garden of Medicinal Plants, Nanning, Guangxi, 530004, P. R. China

Abstract

The binding properties of chrysin with serum albumin (SA) were investigated under physiological conditions by calorimetry, circular dichroism (CD) spectroscopy, and molecular modeling. Based on the thermodynamic data, molar reaction enthalpy, reaction order ( n) and the rate constant ( k) were calculated. The results of CD spectroscopy showed that chrysin could bind to SA and the conformation of SA did not have any high-ordered structural change. Computational mapping revealed chrysin binding to the subdomain IB in SA. The chrysin-serum albumin complex was stabilized by hydrophobic force and hydrogen bonding and the reaction was a spontaneous process.

Publisher

SAGE Publications

Subject

Complementary and alternative medicine,Plant Science,Drug Discovery,Pharmacology,General Medicine

Link

http://journals.sagepub.com/doi/pdf/10.1177/1934578X1400900215

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