Mechamism of action of a potent antiplatelet peptide, triflavin from Trimeresurus flavoviridis snake venom

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

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Triflavin, an antiplatelet peptide from Trimeresurus flavoviridis snake venom, inhibits aggregation of human platelets stimulated by a variety of agonists. However, triflavin does not affect the shape change and release reaction of platelets stimulated by thrombin and collagen. In this paper, we further investigate its effect on the intracellular events occurring after the activation of platelets. Triflavin does not inhibit the intracellular free calcium rise of Quin 2-AM loaded platelets stimulated by thrombin and it also has no significant effect on thromboxane B2 formation of platelets stimulated by thrombin. Triflavin does not affect the 3(H)-inositol monophosphate formation of the 3(H)myoinositol loaded platelets. However, triflavin dose-dependently inhibits fibrinogen-induced aggregation and 125I-fibrinogen binding of ADP-stimulated platelets. In addition, triflavin dose-dependently blocks fibrinogen-induced aggregation of elastase-treated platelets. It is concluded that trifavin specifically inhibits fibrinogen binding to fibrinogen receptors associated with glycoprotein IIb/IIIa complex on platelet membrane surface without any inhibitory effect on the platelet-activation process.

Original languageEnglish
Pages (from-to)489-493
Number of pages5
JournalThrombosis and Haemostasis
Issue number4
Publication statusPublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • Hematology


Dive into the research topics of 'Mechamism of action of a potent antiplatelet peptide, triflavin from Trimeresurus flavoviridis snake venom'. Together they form a unique fingerprint.

Cite this