Antithrombotic Peptides from Scolopendra subspinipes mutilans Hydrolysates

Abstract

The centipedes are a type of traditional Chinese herb and can treat cardiovascular diseases. In this study, we aimed to isolate bioactive peptides from the enzymatic hydrolysates of centipedes. Three novel antithrombotic peptides were isolated from centipedes hydrolysates using a combination of ultrafiltration, Sephadex G-50 column, and RP-HPLC C8 column. The molecular mass of the purified peptides are 753, 515 and 985 Da measured by Electrospray Ionization Mass Spectrometry. The primary structures of these peptides were determined to be Phe-Ser-Ala-Pro-Ala-Val-Tyr (FSAPAVY), Ile-Arg-Asp-Leu (IRDL) and Asp-Leu-Asp-His-Tyr-Ser-Phe (DLDHYSF) using Edman degradation method. All isolated peptides potently prolonged the activated partial thromboplastin time. Moreover, IRDL and DLDHYSF can inhibit platelet aggregation, prolong bleeding time and clotting time. These results indicate that the enzymatic hydrolysate of Scolopendra subspinipes mutilans may contribute to the antithrombotic activity of the centipede for treatment of cardiovascular and cerebrovascular diseases.