Affinity of rosmarinic acid to human serum albumin and its effect on protein conformation stability. (1st February 2016)

• Record Type: Journal Article
• Authors: Peng, Xin; Wang, Xiangchao; Qi, Wei; Su, Rongxin; He, Zhimin
• Is Part Of: Food chemistry. Volume 192(2016)
• Page Start: 178
• Page End: 187
• Publication Date: 2016-02-01
• Subjects: Rosmarinic acid -- Human serum albumin -- Multi-spectroscopic -- Molecular docking -- Molecular dynamics simulation; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2015.06.109
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The interaction mechanism between HSA and RA was investigated in vitro . RA can spontaneously bind to site I of HSA with moderately strong binding affinity through hydrophobic interaction. The conformation of HSA was changed after RA binding. The binding study was also explored by molecular docking and molecular dynamic simulation. Abstract: Rosmarinic acid (RA) is a natural polyphenol contained in many aromatic plants with promising biological activities. The interaction between RA and human serum albumin (HSA) was investigated by multi-spectroscopic, electrochemistry, molecular docking and molecular dynamics simulation methods. The fluorescence emission of HSA was quenched by RA through a combined static and dynamic quenching mechanism, but the static quenching was the major constituent. Fluorescence experiments suggested that RA was bound to HSA with moderately strong binding affinity through hydrophobic interaction. The probable binding location of RA was located near site I of HSA. Additionally, as shown by the Fourier transform infrared (FT-IR) and circular dichroism (CD) spectra, RA can result in conformational and structural alterations of HSA. Furthermore, the molecular dynamics studies were used to investigate the stability of the HSA and HSA–RA system. Altogether, the results can provide an important insight for the applications of RA in the food industry.