Characterization of ACE-Inhibitory Peptide Associated with Antioxidant and Anticoagulation Properties

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 mu M. 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. Keywords: ACE-inhibitory activity, anticoagulation activity, DPPH radical-scavenging activity, egg white, peptide