A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom

T. F. Huang, J. R. Sheu, C. M. Teng

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

The interaction of fibrinogen with its receptors on platelet surfaces leads to platelet aggregation. A snake-venom peptide, trigramin, has previously been demonstrated to inhibit platelet aggregation by acting as a fibrinogen-receptor antagonist. By means of gel filtration, ionic-exchange chromatography and reverse-phase h.p.l.c., a potent platelet-aggregation inhibitor, triflavin, has now been purified from the venom of Trimeresurus flavoviridis. The purified triflavin is a single chain polypeptide, consisting of about 71 amino acid residues with a molecular mass of 7600 Da, and its N-terminal sequence is Gly-Glu-Glu-Cys-Asp. Triflavin dose-dependently inhibited human platelet aggregation stimulated by ADP, adrenaline, collagen, thrombin or prostaglandin endoperoxide analogue U46619 in preparations of platelet-rich plasma, platelet suspension and whole blood. Its IC50 ranged from 38 to 84 nM, depending on the aggregation inducer used and the platelet preparation. However, triflavin apparently did not affect the platelet shape change and ATP-release reactions caused by these agonists. Triflavin inhibited fibrinogen-induced aggregation of human elastase-treated platelets in a dose dependent manner, indicating that it directly interferes with the binding of fibrinogen to its receptors on platelet membranes exposed by elastase treatment. Additionally, triflavin dose-dependently blocked 125 I labelled fibrinogen binding to ADP-activated platelets. In conclusion, triflavin inhibits platelet aggregation through the blockade of fibrinogen binding to fibrinogen receptors on platelet membranes.

Original languageEnglish
Pages (from-to)351-357
Number of pages7
JournalBiochemical Journal
Volume277
Issue number2
Publication statusPublished - 1991
Externally publishedYes

Fingerprint

Trimeresurus
Snake Venoms
Platelets
Blood Platelets
Peptides
Fibrinogen
Platelet Aggregation
Fibrinogen Receptors
Agglomeration
Pancreatic Elastase
Adenosine Diphosphate
Synthetic Prostaglandin Endoperoxides
15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid
Platelet-Rich Plasma
Membranes
triflavin
Platelet Aggregation Inhibitors
Reverse-Phase Chromatography
Thrombin
Epinephrine

ASJC Scopus subject areas

  • Biochemistry

Cite this

A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom. / Huang, T. F.; Sheu, J. R.; Teng, C. M.

In: Biochemical Journal, Vol. 277, No. 2, 1991, p. 351-357.

Research output: Contribution to journalArticle

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