Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 482, Issue 1-2, Pages 25-32Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.11.023
Keywords
Disintegrin; Aggregation; Receptor; Platelet; Inhibitor; RGD-peptide; Integrin; Jarastatin; Jararacin; Molecular modeling
Categories
Funding
- Conselho Nacional de Desenvolvimento Cientifico (CNPq)
- Funda go de Amparo Pesquisa do Estado do Rio de Janeiro (FAPERJ)
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Universidade Federal Fluminense (UFF) (Brazil)
- FAPERJ
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alpha IIb beta 3 is ail 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 alpha IIb beta 3 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. (c) 2008 Elsevier Inc. All rights reserved.
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