Tyrosine-rich conopeptides affect voltage-gated K+ channels

Imperial, Julita S., Chen, Ping, Sporning, Annett, Terlau, Heinrich, Daly, Norelle L., Craik, David J., Alewood, Paul F. and Olivera, Baldormero M. (2008) Tyrosine-rich conopeptides affect voltage-gated K+ channels. The journal of biological chemistry, 283 34: 23026-23032. doi:10.1074/jbc.M800084200

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Author Imperial, Julita S.
Chen, Ping
Sporning, Annett
Terlau, Heinrich
Daly, Norelle L.
Craik, David J.
Alewood, Paul F.
Olivera, Baldormero M.
Title Tyrosine-rich conopeptides affect voltage-gated K+ channels
Journal name The journal of biological chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2008-05-27
Year available 2008
Sub-type Article (original research)
DOI 10.1074/jbc.M800084200
Open Access Status File (Publisher version)
Volume 283
Issue 34
Start page 23026
End page 23032
Total pages 8
Place of publication Baltimore
Publisher American society for Biochemistry and Molecular Biology
Language eng
Subject C1
030401 Biologically Active Molecules
970107 Expanding Knowledge in the Agricultural and Veterinary Sciences
Abstract Two venom peptides, CPY-Pl1 (EU000528) and CPY-Fe1 (EU000529), characterized from the vermivorous marine snails Conus planorbis and Conus ferrugineus, define a new class of conopeptides, the conopeptide Y (CPY) family. The peptides have no disulfide cross-links and are 30 amino acids long; the high content of tyrosine is unprecedented for any native gene product. The CPY peptides were chemically synthesized and shown to be biologically active upon injection into both mice and Caenorhabditis elegans; activity on mammalian Kv1 channel isoforms was demonstrated using an oocyte heterologous expression system, and selectivity for Kv1.6 was found. NMR spectroscopy revealed that the peptides were unstructured in aqueous solution; however, a helical region including residues 12-18 for one peptide, CPY-Pl1, formed in trifluoroethanol buffer. Clones obtained from cDNA of both species encoded prepropeptide precursors that shared a unique signal sequence, indicating that these peptides are encoded by a novel gene family. This is the first report of tyrosine-rich bioactive peptides in Conus venom.
Formatted abstract
Two venom peptides, CPY-Pl1 (EU000528) and CPY-Fe1 (EU000529), characterized from the vermivorous marine snails Conus planorbis and Conus ferrugineus, define a new class of conopeptides, the conopeptide Y (CPY) family. The peptides have no disulfide cross-links and are 30 amino acids long; the high content of tyrosine is unprecedented for any native gene product. The CPY peptides were chemically synthesized and shown to be biologically active upon injection into both mice and Caenorhabditis elegans; activity on mammalian Kv1 channel isoforms was demonstrated using an oocyte heterologous expression system, and selectivity for Kv1.6 was found. NMR spectroscopy revealed that the peptides were unstructured in aqueous solution; however, a helical region including residues 12–18 for one peptide, CPY-Pl1, formed in trifluoroethanol buffer. Clones obtained from cDNA of both species encoded prepropeptide precursors that shared a unique signal sequence, indicating that these peptides are encoded by a novel gene family. This is the first report of tyrosine-rich bioactive peptides in Conus venom.
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
BIOCHEMISTRY & MOLECULAR BIOLOGY
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID GM48667
Forderkennzeichen 0311859
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 16 Apr 2009, 01:27:43 EST by Cody Mudgway on behalf of Institute for Molecular Bioscience