Fluorescence spectroscopy and molecular simulation on the interaction of caffeic acid with human serum albumin. (13th April 2016)

• Record Type: Journal Article
• Authors: Xiang, Yuhong; Duan, Lili; Ma, Qiang; Lv, Zizheng; Ruohua, Zhu; Zhang, Zhuoyong
• Is Part Of: Luminescence. Volume 31:Number 8(2016)
• Page Start: 1496
• Page End: 1502
• Publication Date: 2016-04-13
• Subjects: caffeic acid -- human serum albumin -- fluorescence -- molecular simulations; Luminescence -- Periodicals; Bioluminescence -- Periodicals; Chemiluminescence -- Periodicals; Luminescence -- Periodicals; 535.35
• DOI: 10.1002/bio.3135
• Languages: English
• ISSNs: 1522-7235

Abstract

Abstract: Fluorescence spectroscopy and molecular simulation were explored to study the interaction between caffeic acid and human serum albumin (HSA). The experimental results indicated that the fluorescence quenching mechanism between caffeic acid and HSA is a static quenching, which was proved again by the analysis of fluorescence lifetime by time‐correlated single photon counting. The binding process is spontaneous and the hydrophobic force is the main force between caffeic acid and HSA. In addition, the binding of caffeic acid to HSA was modeled by molecular dynamics simulations. The root mean square deviations, root mean square fluctuations, radius of gyration and the number of hydrogen bonds of the molecular dynamic (MD) simulation process were analyzed. Both experimental and modeling results demonstrated strong binding between HSA and caffeic acid. HSA had a slight conformational change when it binds with caffeic acid. The obtained information is useful for HSA drug design. Copyright © 2016 John Wiley & Sons, Ltd.