Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry (Articolo in rivista)

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  • Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.16/j.bbrc.2007.04.121 (literal)
Alternative label
  • Cabras T., Patamia M., Melino S., Inzitari R., Messana I., Castagnola M., Petruzzelli R. (2007)
    Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry
    in Biochemical and biophysical research communications (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cabras T., Patamia M., Melino S., Inzitari R., Messana I., Castagnola M., Petruzzelli R. (literal)
Pagina inizio
  • 277 (literal)
Pagina fine
  • 284 (literal)
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  • 358 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Tiziana Cabras a, Maria Patamia b, Sonia Melino c, Rosanna Inzitari b, Irene Messana a, Massimo Castagnola b, Raffaele Petruzzelli d, a Dipartimento di Scienze Applicate ai Biosistemi, Universita` di Cagliari, Italy b Istituto di Biochimica e Biochimica Clinica, Facolta` di Medicina and Istituto per la Chimica del Riconoscimento Molecolare, CNR, Universita` Cattolica, Roma, Italy c Dipartimento di Scienze e Tecnologie Chimiche, Universita` di Roma ''Tor Vergata'', Italy d Dipartimento di Scienze Biomediche, Universita` ''G.D'Annunzio'', Chieti, Italy (literal)
Titolo
  • Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry (literal)
Abstract
  • Histatin 5 is a cationic salivary peptide with strong candidacidal and bactericidal activity at physiological concentration. In this paper we demonstrate by optical spectroscopy and ESI-IT-MS experiments that a synthetic peptide related to the N-terminus of histatin 5 specifically binds copper ions in vitro and that the complex metal-peptide generates reactive oxygen species at physiological concentration of ascorbate, leading to significant auto-oxidation of the peptide within short reaction time. The oxidative activity of this peptide is associated to the presence of a specific metal binding site present at its N-terminus. The motif is constituted by the amino acid sequence NH2-Asp-Ser-His, representing a copper and nickel amino terminal binding site, known as ''ATCUN motif''. The results of the study suggest that the production of reactive oxygen species can be an intrinsic property of histatin 5 connected to its ability to bind metals. (literal)
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