Identification and molecular interactions of novel ACE inhibitory peptides from rapeseed protein

Plant-derived bioactive peptides have drawn much attention because of their physiological functions. This study aimed to evaluate bioactive peptides in rapeseed protein and identify novel angiotensin I-converting enzyme (ACE) inhibitory peptides using bioinformatics methods. A total of 24 kinds of bioactive peptides were encrypted in the 12 selected rapeseed proteins by analysis in BIOPEP-UWM, with higher occurrence frequency of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides (0.5727-0.7487) and ACE inhibitory peptides (0.3500-0.5364). Novel ACE inhibitory peptides FQW, FRW and CPF were identified by in silico proteolysis, and they had strong inhibitory effects on ACE in vitro, showing IC50 values of 44.84 +/- 1.48 mu M, 46.30 +/- 1.39 mu M and 131.35 +/- 3.87 mu M, respectively. Molecular docking results displayed that these three peptides were able to interact with ACE active site via hydrogen bonds and hydrophobic interactions, and coordinate with Zn2+. It suggested that rapeseed protein could be a good source for the production of ACE inhibitory peptides.

Automated summary

Plant-derived bioactive peptides, particularly ACE inhibitory peptides, were evaluated in rapeseed protein. The study identified novel ACE inhibitory peptides FQW, FRW, and CPF using bioinformatics methods. In vitro experiments showed that these peptides exhibited strong inhibitory effects on ACE, indicating that rapeseed protein can be a good source for ACE inhibitory peptides.