Anticancer Activity of an Oligopeptide Isolated from Hydrolysates of Sepia Ink

AimTo investigate the antitumor effect of peptides from Sepia ink by enzymatic hydrolysis.MethodsSepia ink was hydrolyzed with trypsin to prepare peptides; hydrolysates were isolated by ultrafiltration and purified using G-25 gel filtration. The purity of the sepia ink oligopeptides was demonstrated by HPLC and its peptide sequence was detected. Then CCK-8 method was employed to measure cellular viability, and HE staining was used to detect cell morphological change.ResultsAn oligopeptide was obtained from the hydrolysates of Sepia ink and identified as N Gln-Pro-Lys with a molecular mass of 343.4. The yield of oligopeptides was 1.82%. The CCK-8 assay showed that N Gln-Pro-Lys significantly inhibited the proliferation of DU-145 cells and induced their death in a dose-dependent manner. The morphologic changes were observed by HE staining after treated with sepia ink oligopeptides.ConclusionN Gln-Pro-Lys showed potent antitumor activity.