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Identification of tyrosine sulfation in Conus pennaceus conotoxins alpha-PnIA and alpha-PnIB: further investigation of labile sulfo- and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atmospheric pressure MALDI mass spectrometry.
Wolfender, J L; Chu, F; Ball, H; Wolfender, F; Fainzilber, M; Baldwin, M A; Burlingame, A L.
Afiliação
  • Wolfender JL; Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
J Mass Spectrom ; 34(4): 447-54, 1999 Apr.
Article em En | MEDLINE | ID: mdl-10226369
Liquid chromatography/electrospray ionization mass spectrometry was used to investigate the peptide composition of the venom of Conus pennaceus, a molluscivorous cone shell from the Red Sea. Based on observed M(r)s, this venom contained all known conotoxins previously isolated and identified from this species. Interestingly, the doubly protonated species of only two of these conotoxins, alpha-PnIA and alpha-PnIB, showed additional related ions at +40 m/z (+80 Da), indicating the presence of either sulfation or phosphorylation in both components. High-performance liquid chromatographic (HPLC) fractions containing these two conotoxins were examined by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry in both positive and negative ion modes, as well as by MALDI high-energy collision-induced dissociation. These experiments established the presence of a single sulfated tyrosine residue within both alpha-PnIA and alpha-PnIB. Hence their post-translationally modified sequences are GCCSLPPCAANNPDY(S)C-NH2 (alpha-PnIA) and GCCSLPPCALSNPDY(S)C-NH2 (alpha-PnIB). This assignment was supported by comparison of their mass spectral behavior with that of known sulfated and phosphorylated peptides. This data clarified further the distinguishing features of the ionization and fragmentation of such modified peptides. Selective disulfide folding of synthetic alpha-PnIB demonstrated that both sulfated and non-sulfated toxins co-elute on reversed-phase HPLC and that alpha-PnIB possesses the same disulfide connectivity as other 'classical' alpha-conotoxins reported previously.
Assuntos
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Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Espectrometria de Massas / Conotoxinas Idioma: En Ano de publicação: 1999 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Espectrometria de Massas / Conotoxinas Idioma: En Ano de publicação: 1999 Tipo de documento: Article