Screening of Monoamine Oxidase A Inhibitory Peptides from Proteins of Edible Fungi

Abstract In this paper, the binding relationship between oligopeptides of edible fungi and monoamine oxidase A (MAO-A) was explored by computer simulation. The frequency of high affinity oligopeptides (F value) was calculated, and the MAO-A inhibitory peptide was screened. By simulating the hydrolysis of 27 proteins from 8 common edible fungi in China, the oligopeptides obtained by hydrolysis were docked with MAO-A to screen high affinity oligopeptides (docking fraction ≤ -120) and ultra-high affinity oligopeptides (docking fraction ≤ -160). At the same time, the F value was calculated to predict the inhibitory effect of edible fungi protein on MAO-A. A total of 430 high-affinity oligopeptides and 32 ultra-high-affinity oligopeptides were obtained by molecular docking after 27 proteins were simulated hydrolysis. Among them, the three oligopeptides with the highest docking were PQSTW (-195.952), PTSGW (-187.942) and QCQW (-180.007). In addition, the simulated hydrolyzed edible fungi all contained oligopeptides with strong inhibitory effect on MAO-A. In summary, this paper aims to screen MAO-A inhibitory peptides, provide new possibilities for high-speed screening of MAO-A inhibitory peptides, and provide a theoretical basis for exploring the potential value of edible fungi.