title: Molecular interactions of flavonoids to pepsin: Insights from spectroscopic and molecular docking studies.
abstract: In the work described on this paper, the inhibitory effect of 10 flavonoids on pepsin and the interactions between them were investigated by a combination of spectroscopic and molecular docking methods. The results indicated that all flavonoids could bind with pepsin to form flavonoid-pepsin complexes. The binding parameters obtained from the data at different temperatures revealed that flavonoids could spontaneously interact with pepsin mainly through electrostatic forces and hydrophobic interactions with one binding site. According to synchronous and three-dimensional fluorescence spectra and molecular docking results, all flavonoids bound directly into the enzyme cavity site and the binding influenced the microenvironment and conformation of the pepsin activity site which resulted in the reduced enzyme activity. The present study provides direct evidence at a molecular level to understand the mechanism of digestion caused by flavonoids.
authors.affiliation: School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, PR China.
authors.forename: Hua-Jin
authors.initials: HJ
authors.lastname: Zeng
authors.affiliation: College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, PR China. Electronic address: yangran@zzu.edu.cn.
authors.forename: Ran
authors.initials: R
authors.lastname: Yang
authors.affiliation: School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, PR China.
authors.forename: Huili
authors.initials: H
authors.lastname: Liang
authors.affiliation: College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, PR China; School of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou 450001, PR China.
authors.forename: Ling-Bo
authors.initials: LB
authors.lastname: Qu
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D002942:Circular Dichroism; D005419:Flavonoids / Q000737:chemistry* / Q000378:metabolism*; D005453:Fluorescence; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D015394:Molecular Structure; D010434:Pepsin A / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
chemical_list: D005419:Flavonoids; D010434:Pepsin A
keywords: Flavonoid; Fluorescence spectroscopy; Interaction; Molecular docking; Pepsin