Identification and functional analysis of a novel bradykinin inhibitory peptide in the venoms of New World Crotalinae pit vipers

Graham, Robert Leslie James and Graham, Ciaren and McClean, Stephen and Chen, Tianbao and O'Rourke, Martin and Hirst, David and Theakson, David and Shaw, Chris (2005) Identification and functional analysis of a novel bradykinin inhibitory peptide in the venoms of New World Crotalinae pit vipers. Biochemical and Biophysical Research Communications, 338 (3). pp. 1587-1592. ISSN 0006-291X

Full content URL: http://dx.doi.org/10.1016/j.bbrc.2005.10.130

Full text not available from this repository.

Item Type:Article
Item Status:Live Archive

Abstract

A novel undecapeptide has been isolated and structurally characterized from the venoms of three species of New World pit vipers from the subfamily, Crotalinae. These include the Mexican moccasin (Agkistrodon bilineatus), the prairie rattlesnake (Crotalus viridis viridis), and the South American bushmaster (Lachesis muta). The peptide was purified from all three venoms using a combination of gel permeation chromatography and reverse-phase HPLC. Automated Edman degradation sequencing and MALDI-TOF mass spectrometry established its peptide primary structure as: Thr-Pro-Pro-Ala-Gly-Pro-Asp-Val-Gly-Pro-Arg-OH, with a non-protonated molecular mass of 1063.18 Da. A synthetic replicate of the peptide was found to be an antagonist of bradykinin action at the rat vascular B2 receptor. This is the first bradykinin inhibitory peptide isolated from snake venom. Database searching revealed the peptide to be highly structurally related (10/11 residues) with a domain residing between the bradykinin-potentiating peptide and C-type natriuretic peptide domains of a recently cloned precursor from tropical rattlesnake (Crotalus durissus terrificus) venom gland. BIP thus represents a novel biological entity from snake venom.

Keywords:Snake Venom, Peptides, Mass Spectrometry, HPLC, Edman degradation sequencing
Subjects:C Biological Sciences > C560 Biotechnology
Divisions:College of Science > School of Life Sciences
ID Code:7334
Deposited On:22 Jan 2013 12:39

Repository Staff Only: item control page