Study on the binding of chlorogenic acid to pepsin by spectral and molecular docking

Abstract

The interaction of pepsin with chlorogenic acid (CHA) was investigated using fluorescence, UV/vis spectroscopy and molecular modeling methods. Stern-Volmer analysis indicated that the fluorescence quenching of pepsin by CHA resulted from a static mechanism, and the binding constant was 1.1846 × 10(5) and 1.1587 × 10(5) L/mol at 288 and 310 K, respectively. The distance between donor (pepsin) and acceptor (CHA) was calculated to be 2.39 nm and the number of binding sites for CHA binding on pepsin was ~ 1. The results of synchronous fluorescence and three-dimensional fluorescence showed that binding of CHA to pepsin could induce conformational changes in pepsin. Molecular docking experiments found that CHA bonded with pepsin in the area of the hydrophobic cavity with Van der Waals' forces or hydrogen bonding interaction, which were consistent with the results obtained from the thermodynamic parameter analysis. Furthermore, the binding of CHA can inhibit pepsin activity in vitro.

Interaction Behavior Between Niclosamide and Pepsin Determined by Spectroscopic and Docking Methods

“…in the binding between NIC and pepsin. Results from the present study and other reports showed that binding of many small molecules pepsin occurred via a static quenching mechanism [7,10,11,[36][37][38]. Notably, Li Zhen et al studied the binding between pepsin and nucleoside analogs (FNC, CYD, and CMP) via a static quenching mechanism.…”

“…Curcumin [7] binding with pepsin mainly through hydrophobic interactions with one binding site, while pepsin bind with silybin [10], and nobilietin [37] mainly through hydrophobic and electrostatic interactions. Chlorogenic acid [38] and pepsin were mainly strengthened by Van der Waals' forces and hydrogen bonds. Furthermore, the binding affinity or binding constants varied.…”

Interaction between azo dye Acid Red 14 and pepsin by multispectral methods and docking studies

“…3D fluorescence spectroscopy has been widely used in fluorescence analysis in recent years because it can provide detailed information of the conformational and microenvironmental changes of proteins combining with small molecules . Figure (c, d) shows the 3D fluorescence spectra of pepsin alone and in complex with AR14, respectively.…”

Investigation on the Interaction of Norgestrel with Human Serum Albumin Using Spectroscopy and Molecular‐Docking Method

“…For macromolecules, fluorescence measurements can provide some information on the binding of small molecules with protein, such as the binding mechanism, binding mode, binding constants, binding sites, and intermolecular distances. A variety of molecular interactions can result in quenching, including excited state reactions, molecular rearrangements, energy transfer, and ground-state complex formation [15,16]. Fluorescence-quenching mechanisms generally include static and dynamic quenching [17].…”