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

Abstract : 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.
Document type :
Journal articles
Complete list of metadatas

https://hal.archives-ouvertes.fr/hal-00521834
Contributor : Isabelle Frapart <>
Submitted on : Tuesday, September 28, 2010 - 4:14:53 PM
Last modification on : Tuesday, June 4, 2019 - 4:30:10 PM

Links full text

Identifiers

Collections

Citation

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, Wiley-Blackwell, 2009, 44 (1), pp.81-89. ⟨10.1002/jms.1473⟩. ⟨hal-00521834⟩

Share

Metrics

Record views

79