Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

• Published in: Luminescence (Chichester, England) Vol. 37; no. 6; pp. 1025 - 1036
• Main Authors: Nai, Xiao, Chen, Yanrong, Zhang, Qian, Hao, Shengyu, Xuan, Hongzhuan, Liu, Jie
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01.06.2022
• Subjects: Affinity; Analytical methods; Antitumor agents; Binding; Caffeic acid; caffeic acid phenethyl ester (CAPE); Chymotrypsin; Circular dichroism; Design modifications; Dichroism; Drug development; Enthalpy; Fluorescence; Free radicals; Hydrogen bonds; Light scattering; Metabolism; Molecular docking; Pepsin; Photon correlation spectroscopy; Protease; Protein structure; Proteinase; Secondary structure; Spectroscopy; Trypsin; Ultraviolet spectroscopy; α‐chymotrypsin; trypsin; caffeic acid phenethyl ester (CAPE); α-chymotrypsin; pepsin
• ISSN: 1522-7235; 1522-7243
• DOI: 10.1002/bio.4262

The interaction of one anticancer drug (caffeic acid phenethyl ester; CAPE) with three proteases (trypsin, pepsin and α‐chymotrypsin) has been investigated with multispectral methods and molecular docking. As an active components in propolis, the findings are of great benefit to metabolism, design, and structural modification of drugs. The results show that CAPE has an obvious ability to quench the trypsin, pepsin, or α‐chymotrypsin fluorescence mainly through a static quenching procedure. Trypsin has the largest binding affinity to CAPE, and α‐chymotrypsin has the smallest binding affinity to CAPE. The data obtained from thermodynamic parameters and molecular docking prove that the spontaneously interaction between CAPE and each protease is mainly due to a combination of van der Waals (vdW) force and hydrogen bond (H‐bond), controlled by an enthalpy‐driven process. The binding force, strength, position, and the number of H‐bond are further obtained from the results of molecular docking. Through ultraviolet spectroscopy, dynamic light scattering and circular dichroism experiments, the change in the protease secondary structure induced by CAPE was observed. Additionally, the addition of protease had a positive effect on the antioxidative activity of CAPE, and α‐chymotrypsin has the greatest effect on the removal of 2,2‐diphenyl‐1‐picrylhydrazyl free radicals by CAPE. The interaction of CAPE with protease has been investigated with multispectral methods and molecular docking. CAPE has the strongest binding affinity to Try and the smallest binding affinity to Pep. The interaction forces are vdW force and H‐bond.