Purification and characterization of a novel antithrombotic peptide from Scolopendra subspinipes mutilans

J Ethnopharmacol. 2013 Jan 9;145(1):182-6. doi: 10.1016/j.jep.2012.10.048. Epub 2012 Nov 2.

Abstract

Ethnopharmacological relevance: The centipede has been prescribed for the treatment of cardiovascular diseases in Korea, China and other Far Eastern Asian countries for several hundred years.

Materials and methods: A novel antithrombotic peptide was isolated from Scolopendra subspinipes mutilans using a combination of ultrafiltration, Sephadex G-50 column, Source 15Q anion exchange column and RP-HPLC C18 column.

Results: The molecular mass of the purified peptide is 346Da measured by Electrospray Ionization Mass Spectrometry (ESI-MS). The primary structure of the peptide is Ser-Gln-Leu (SQL) determined by Edman degradation. SQL potently prolonged the activated partial thromboplastin time (aPTT), and inhibited platelet aggregation.

Conclusions: These results help to clarify the mechanism of the antithrombotic activity of the centipede for effective treatment of cardiovascular and cerebrovascular diseases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropods / chemistry*
  • Fibrinolytic Agents / chemistry
  • Fibrinolytic Agents / isolation & purification*
  • Fibrinolytic Agents / pharmacology*
  • Molecular Weight
  • Partial Thromboplastin Time / methods
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Peptides / pharmacology*
  • Platelet Aggregation / drug effects
  • Prothrombin Time / methods

Substances

  • Fibrinolytic Agents
  • Peptides