A bioactive peptide Arg–Val–Pro–Ser–Leu (RVPSL) obtained from egg white protein was characterized by
LC-MS and further chemically synthesized by the Fmoc solid phase method and investigated in terms of its angiotensin
converting enzyme (ACE)-inhibitory activity, antioxidant property, and anticoagulation activity, as well as its stability in a
simulated gastrointestinal digestion. The peptide exhibited an ACE-inhibitory activity with an IC50 value of 20 μM. Also,
the peptide could efficiently quench the (1,1)-diphenyl-2-picrylhydrazyl free radicals and exhibit high anticoagulation
activity with a complete inhibition at 100 mM. Moreover, the peptide has a good stability against protease digestion.
These results suggest that the peptide RVPSL may have potential to be used in nutraceuticals and functional food.