Computer Simulation for Screening Protease Activated Receptor 2 Inhibitory Peptides Derived from Edible Algal Proteins
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Abstract:
Computer simulations were used to predict the bioactive peptides inhibiting protease activated receptor 2 (PAR2) from food source proteins, as well as the bioactivity, water solubility, and other physicochemical parameters of the peptides obtained from the enzymatic digestion of edible algal proteins. First, edible algal proteins were selected from the NCBI database and Protein Data Bank (PDB). Thereafter, enzymatic digestion was simulated using the BIOPEP-UWM database, activity analysis was performed using Peptide Ranker, high active peptides were predicted using Innovagen and ToxinPred, and finally, HPEPDOCK was used. The obtained small active peptides with activity scores over 0.5, excellent water solubility, and non-toxicity were simulated by molecular docking using PAR2 to investigate their molecular binding ability. The potential and mechanism to discriminate different small active peptides to inhibit PAR2 activity was analyzed. The results showed that the small molecule oligopeptides PAGR (-165.80), PAR (-163.93), IDQW (-152.95) and DISAW (-154.48) exhibited high binding to PAR2 and were potential active inhibitory peptides of PAR2. The findings of this study provide valuable insights for developing and utilizing algal proteins and exploring PAR2 inhibitors.
