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Bradykinin-related peptides from Phyllomedusa hypochondrialis azurea: mass spectrometric structural characterisation and cloning of precursor cDNAs

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

Thompson, Alan Hunter, Bjourson, AJ, Shaw, Chris and McClean, Stephen (2006) Bradykinin-related peptides from Phyllomedusa hypochondrialis azurea: mass spectrometric structural characterisation and cloning of precursor cDNAs. RAPID COMMUNICATIONS IN MASS SPECTROMETRY, 20 (24). pp. 3780-3788. [Journal article]

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DOI: 10.1002/rcm.2791

Abstract

Amphibian skin secretions contain a plethora of bioactive compounds, many of which are understood to act to deter ingestion by predators. Bradykinins in particular are constitutively expressed in many amphibian skin secretions, mediating a variety of effects including hyperalgesia and contraction of gastric smooth muscle. Using a variety of proteomic techniques (high-performance liquid chromatography (HPLC) separation, matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOFMS), and quadrupole time-of-flight tandem mass spectrometry (Q-TOF-MS/MS)) the current study identified 13 bradykinin-like peptides in the skin secretions of Phyllomedusa hypochondrialis azurea, including several new C-terminally extended isoforms (VPPGFTPFRLT, VHypPGFTPFRQT) and a novel phyllokinin-like peptide (RPPGFTPFRVY). Identification of the cDNA sequences encoding these peptides led to the deduction that the peptides were derived from differential post-translational processing and modification of five different precursors. Such an event emphasises the metabolic efficiency of peptide production in amphibian venom, with multiple products perhaps selective to different receptors in a variety of predators generated from a single precursor. An unusual modification was also recognised in the present study, with several bradykinin-like peptides featuring hydroxyprolination of the first proline residue rather than the commonly targeted second. This alteration may be mediated by the structural organisation of N-terminal amino acids prior to precursor processing. Copyright (c) 2006 John Wiley & Sons, Ltd.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Pharmaceutical Science and Practice
Biomedical Sciences Research Institute > Stratified Medicine
ID Code:1927
Deposited By:Mrs Caroline Adams
Deposited On:30 Nov 2009 09:25
Last Modified:14 Oct 2013 15:45

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