Bradykinin potentiating peptides of venoms: review article
2009
Omar, H.El.
Animal kingdom possesses numerous species that produce toxins. Snakes and scorpion possess the most diverse animal toxins in the animal kingdom. That exert different functions. Bradykinin is a nonapeptide with the amino acid sequence: Arg-Pro-proGly-Phe-Ser-Pro-Phe-Arg. This peptide is cleaved from a2 globulin that is synthesized by the liver and circulate in the plasma. It exerts potent biological effect in a variety of organs and tissues. Bradykinin potentiating peptides (BPPs) are pyroglutamyl proline rich in oligopolypeptides. BPPs isolated from Bothrops jararaca venom were described in the middle of 1960s as a first natural inhibitors of the angiotensin converting enzyme. The chemical and pharmacological properties of BPPs were essential for the Captopril, the first active site directed inhibitors of angiotensin converting enzyme used to treat human hypertension. Among the 18 natural peptides whose sizes vary between 5 and 14 amino acids, the most potent is BPPsa (Gin, Lys, Trp, Ala, Pro) and BPP9a (Glu, Trp, Pro, Arg, Pro, Gin, lie, Pro, Pro). BPPs are larger than seven amino acid residues share similar features including high content of proline residues and tripeptide Ile-Pro-Pro at the C-terminus. Recently, the molecular biology of the BPPs revealed that they are part of two distinct C-type natriuretic peptide precursors found in the venom gland and the brain of Bothrops jararaca, each containing seven BPPs. These peptides have been used as probes selective tools in the study of physiological processes and in the development of therapeutic agents. Therefore, BPPs hold great promise in the future understanding and treatment of cardiovascular disease.
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