Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay

Abstract

Abstract A complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from egg white ovalbumin. The sequence of the protein was initially obtained from the NCBI database followed by in silico digestion using different enzymes or combination of enzymes. The results showed that 71 peptides were produced. Their bioactivities were then predicted based on the amino acid compositions and sequences as well as the peptide interactions with ACE and DPP-4. Ten highly potential peptides (CF, KM, ELPF, AM, ADHPF, LPR, PR, FR, PRM and GR) were chosen as they obtained p-value less than 0.01. The results from the in vitro validation experiment showed that all peptides were able to inhibit the ACE and DPP-4. Overall, this study underlined the in silico approach as an alternative way for bioactive peptide discovery which could tremendously reduce the cost and time of research.