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Histidine‐rich peptide: evidence for a single zinc‐binding site on H5WYG peptide that promotes membrane fusion at neutral pH
Author(s) -
Buré Corinne,
Maget Régine,
Delmas Agnès F.,
Pichon Chantal,
Midoux Patrick
Publication year - 2009
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1473
Subject(s) - chemistry , peptide , mass spectrometry , zinc , histidine , tandem mass spectrometry , electrospray ionization , membrane , metal ions in aqueous solution , electrospray , metal , inorganic chemistry , chromatography , ion , organic chemistry , biochemistry , amino acid
The histidine‐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 Zn 2+ 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 Zn 2+ 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 Zn 2+ equivalent, correspond to a monomolecular H5WYG − Zn 2+ 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. Copyright © 2008 John Wiley & Sons, Ltd.