Interaction of phenolic acids with trypsin: Experimental and molecular modeling studies.
Trypsin is a kind of protease for digestion and food processing, whose activity can be inhibited by phenolic acids in plant foods. However, most reports explained the inhibitory difference of phenolic acids based on the number and position of substituent groups, which failed to reveal the comprehensive inhibitory mechanism. In this work, the inhibitory effects of 11 common phenolic acids on trypsin were investigated. Amongst the tested cinnamic and benzoic acid derivatives, caffeic acid and gallic acid showed the strongest anti-trypsin activity with a noncompetitive inhibition pattern, respectively. The fluorescence analysis displayed that both the quenching rate constant (Kq) and binding constant (KA) of caffeic acid were higher than those of gallic acid. Molecular docking illustrated their different binding modes with trypsin. The ONIOM calculations revealed that the binding capacity of caffeic acid was higher than that of gallic acid, which could explain their difference in their inhibitory behaviors.
School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
Benguo
B
Liu
Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, PR China.
Huizhi
H
Xiao
Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, PR China.
Jiaqi
J
Li
School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
Sheng
S
Geng
School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
Hanjun
H
Ma
Key Laboratory of Biorheological Science and Technology, Ministry of Education, School of Bioengineering, Chongqing University, Chongqing 400044, PR China. Electronic address: gzliang@cqu.edu.cn.
Guizhao
G
Liang
D062385:Hydroxybenzoates / Q000737:chemistry*; D008958:Models, Molecular; D062105:Molecular Docking Simulation / Q000379:methods*; D014357:Trypsin / Q000737:chemistry*
D062385:Hydroxybenzoates; D014357:Trypsin; C017616:phenolic acid
Inhibition; Molecular docking; ONIOM (our Own N-layer Integrated Orbital molecular Mechanics) calculations; Phenolic acid; Trypsin