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. (c) 2007 Elsevier Inc. All rights reserved.

Cabras, T., Patamia, M., Melino, S.m., Inzitari, R., Messana, I., Castagnola, M., et al. (2007). Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 358(1), 277-284 [10.1016/j.bbrc.2007.04.121].

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

MELINO, SONIA MICHAELA;
2007-01-01

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. (c) 2007 Elsevier Inc. All rights reserved.
2007
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
ATCUN" motif; ESI-IT-MS spectrometry; Histatin 5; Metals; Reactive oxygen species (ROS)"
Cabras, T., Patamia, M., Melino, S.m., Inzitari, R., Messana, I., Castagnola, M., et al. (2007). Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 358(1), 277-284 [10.1016/j.bbrc.2007.04.121].
Cabras, T; Patamia, M; Melino, Sm; Inzitari, R; Messana, I; Castagnola, M; Petruzzelli, R
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/34035
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