Purification of a Novel Anticancer Peptide from Enzymatic Hydrolysate of Mytilus coruscus

Abstract

We applied enzymatic hydrolysis and tangential flow filtration (TFF) to purify a novel anticancer peptide from Mytilus coruscus (M. coruscus) and investigated its anticancer properties. To prepare the peptide, eight proteases were employed for enzymatic hydrolysis. Pepsin hydrolysates, which showed clearly superior cytotoxic activity on prostate cancer cells, were further purified using a flow filtration system using a TFF and consecutive chromatographic methods. Finally, a novel anticancer peptide was obtained, and the sequence was identified as Ala-Phe-Asn-Ile-His- Asn-Arg-Asn-Leu-Leu. The peptide from M. coruscus effectively induced cell death on prostate, breast and lung cancer cells but not on normal liver cells. This is the first report of an anticancer peptide derived from the hydrolysates of M. coruscus.