Linked Life Data

14971903

Source:http://linkedlifedata.com/resource/pubmed/id/14971903

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pubmed-article:14971903pubmed:abstractTextAn LC/MS analysis with diagnostic screening for the detection of peptides with posttranslational modifications revealed the presence of novel sulfated peptides within the alpha-conotoxin molecular mass range in Conus anemone crude venom. A functional assay of the extract showed activity at several neuronal nicotinic acetylcholine receptors (nAChRs). Three sulfated alpha-conotoxins (AnIA, AnIB, and AnIC) were identified by LC/MS and assay-directed fractionation and sequenced after purification. The most active of these, alpha-AnIB, was further characterized and used to investigate the influence of posttranslational modifications on affinity. Synthetic AnIB exhibited subnanomolar potency at the rat alpha3beta2 nAChR (IC50 0.3 nM) and was 200-fold less active on the rat alpha7 nAChR (IC50 76 nM). The unsulfated peptide [Tyr16]AnIB showed a 2-fold and 10-fold decrease in activities at alpha3beta2 (IC50 0.6 nM) and alpha7 (IC50 836 nM) nAChR, respectively. Likewise, removal of the C-terminal amide had a greater influence on potency at the alpha7 (IC50 367 nM) than at the alpha3beta2 nAChR (IC50 0.5 nM). Stepwise removal of two N-terminal glycine residues revealed that these residues affect the binding kinetics of the peptide. Comparison with similar 4/7-alpha-conotoxin sequences suggests that residue 11 (alanine or glycine) and residue 14 (glutamine) constitute important determinants for alpha3beta2 selectivity, whereas the C-terminal amidation and sulfation at tyrosine-16 favor alpha7 affinity.lld:pubmed
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pubmed-article:14971903pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:14971903pubmed:articleTitleChemical and functional identification and characterization of novel sulfated alpha-conotoxins from the cone snail Conus anemone.lld:pubmed
pubmed-article:14971903pubmed:affiliationInstitute for Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia.lld:pubmed
pubmed-article:14971903pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:14971903pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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