Key result
Egg white-derived peptide RVPSL inhibits ACE with an IC50 of ~20 μM.
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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 IC(50) 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. Practical Application: The present research revealed a novel multifunctional peptide hydrolyzed from egg white protein. The peptide RVPSL was not only able to block the amplification of the coagulation cascade, but also able to inhibit ACE activity.
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Yu et al. (2011) studied this question. RVPSL peptide was evaluated on ACE-inhibitory and anticoagulation activity. The bioactive peptide RVPSL from egg white protein demonstrated ACE-inhibitory activity with an IC50 of 20 μM and complete inhibition of anticoagulation at 100 mM.
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