title: Affinity of rosmarinic acid to human serum albumin and its effect on protein conformation stability.
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.
authors: School of Life Sciences, Tianjin University, Tianjin 300072, PR China; State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China.
authors: Xin
authors: X
authors: Peng
authors: State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China.
authors: Xiangchao
authors: X
authors: Wang
authors: State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China; Collaborative Innovation Center of Chemistry Science and Engineering (Tianjin), Tianjin 300072, PR China. Electronic address: qiwei@tju.edu.cn.
authors: Wei
authors: W
authors: Qi
authors: State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China; Collaborative Innovation Center of Chemistry Science and Engineering (Tianjin), Tianjin 300072, PR China.
authors: Rongxin
authors: R
authors: Su
authors: State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China; Collaborative Innovation Center of Chemistry Science and Engineering (Tianjin), Tianjin 300072, PR China.
authors: Zhimin
authors: Z
authors: He
mesh_terms: D002934:Cinnamates / Q000737:chemistry*; D002942:Circular Dichroism; D053630:Depsides / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011487:Protein Conformation; D055550:Protein Stability; D012709:Serum Albumin / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics; D000097123:Rosmarinic Acid
chemical_list: D002934:Cinnamates; D053630:Depsides; D012709:Serum Albumin; D000097123:Rosmarinic Acid
keywords: Human serum albumin; Molecular docking; Molecular dynamics simulation; Multi-spectroscopic; Rosmarinic acid