Purification and characterization of a novel anticancer peptide derived from Ruditapes philippinarum

The aim of this study was to purify a novel peptide from Ruditapes philippinarum and investigate its anticancer activities. For the aim, eight proteases were applied for enzymatic hydrolysis. α-Chymotrypsin hydrolyzates, which showed clearly superior cytotoxicity activity on prostate cancer cells, were further purified using a flow filtration system and consecutive chromatographic methods. Finally, a novel anticancer peptide was purified, and the sequence was identified as Ala-Val-Leu-Val-Asp-Lys-Gln-Cys-Pro-Asp at N-terminal. The peptide from R. philippinarum effectively induced apoptosis on prostate, breast and lung cancer cells but not on normal liver cells. This is the first report of an anticancer peptide purified from the hydrolyzates of R. philippinarum.