Histidine-rich peptide: evidence for a single zinc-binding site on H5WYG peptide that promotes membrane fusion at neutral pH - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Mass Spectrometry Année : 2009

Histidine-rich peptide: evidence for a single zinc-binding site on H5WYG peptide that promotes membrane fusion at neutral pH

Résumé

The histicline-rich peptide H5WYG (GLFHAIAHFIHGGWHGLIHGWYG) was found to induce membrane fusion at physiologic pH in the presence of zinc chloride. in this study, we examined the ion selectivity of the interaction of Zn2+ with H5WYG. This investigation was conducted by using adsorption at air/water interface and mass spectrometry. We found that a peptide-metal complex is formed with Zn2+ ions. Electrospray ionisation-mass spectrometry (ESI-MS) reveals that the [H5WYG + Zn + 2H](4+), [H5WYG + Zn + H](3+) and [H5WYG + Zn](2+) ions, appearing by increasing the amount of Zn2+ equivalent, correspond to a monomolecular H5WYG-Zn2+ complex. Tandem mass spectrometry (MS/MS) provides evidence for the binding of the single Zn 2+ ion to the H-11 and H-19 and probably H-15 residues.

Dates et versions

hal-00521834 , version 1 (28-09-2010)

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Citer

Corinne Bure, Régine Maget, Agnès F. Delmas, Chantal Pichon, Patrick Midoux. Histidine-rich peptide: evidence for a single zinc-binding site on H5WYG peptide that promotes membrane fusion at neutral pH. Journal of Mass Spectrometry, 2009, 44 (1), pp.81-89. ⟨10.1002/jms.1473⟩. ⟨hal-00521834⟩
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