Correlation Engine 2.0
Clear Search sequence regions

alphaIIbbeta3 is an integrin that is involved in platelet adhesion and aggregation. This receptor may be inhibited by cysteine-rich peptides known as disintegrins. We isolated two disintegrins from Bothrops jararaca venom called jarastatin and jararacin. We evaluated the structural characteristics and the effects on human platelet aggregation of these disintegrins. Inhibitory profiles were compared to six distinct peptides synthesized based on their RGD hairpin loop primary sequences. Both jarastatin and jararacin inhibited ADP and thrombin induction. Conversely, none of the cyclic peptides showed high-quality activity in assays induced by ADP or thrombin. We constructed homology models for all of these molecules, and theoretically evaluated their interaction with the alphaIIbbeta3 crystal structure using a molecular modeling approach. These results support the observations that the cyclic peptides had little effects, and also reinforce the observation that residues outside the disintegrin RGD sequence are required for interactions with receptor.


Luciana S Wermelinger, Reinaldo B Geraldo, Flavia S Frattani, Carlos R Rodrigues, Maria A Juliano, Helena C Castro, Russolina B Zingali. Integrin inhibitors from snake venom: exploring the relationship between the structure and activity of RGD-peptides. Archives of biochemistry and biophysics. 2009 Feb;482(1-2):25-32

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 19101499

View Full Text