Molecular recognition of angiotensin converting enzyme by snake venom bradykinin potentiating peptides

A. Munawar, A. I. Durrani, H. Ajaz, A. K. Durrani

Abstract


Snake venom is a complex mixture of pharmacologically interesting molecules. In a previous work we isolated and identified bradykinin potentiating peptides (BPP) from the venoms of Bothrops Jararacussu, Vipera ammodytes meridionali and Naja mossambica mossambica. These bradykinin potentiating peptides are inhibitors of angiotensin converting enzyme (ACE). ACE plays a key role in the blood pressure regulation, as part of the renin-angiotensin system. The molecular modelling and docking studies of snake venom bradykinin potentiating peptides, with C-domain human angiotensin converting enzyme, give insights into the protein-ligand interactions, at the active site. These structural studies reveal new binding pockets of the enzyme, which can be used to design new drugs. The study of these interactions can lead to the synthesis of new blood pressure controlling medicine with fewer side effects.


Keywords


Snake venom, bradykinin potentiating peptides, angiotensin converting enzyme, molecular modelling and docking studies, SYBYL-X

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