Histidine-rich peptide: evidence for a single zinc-binding site on H5WYG peptide that promotes membrane fusion at neutral pH.
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.
Buré
Corinne
C
Centre de Biophysique Moléculaire CNRS UPR4301 affiliated to the University of Orléans and Inserm, Orléans cedex 2, France. c.bure@iecb.u-bordeaux.fr
Maget
Régine
R
Delmas
Agnès F
AF
Pichon
Chantal
C
Midoux
Patrick
P
D000327:Adsorption; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008561:Membrane Fusion; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods; D015032:Zinc / Q000737:chemistry / Q000378:metabolism*
C112056:H5WYG peptide; D010455:Peptides; D006639:Histidine; D003300:Copper; D015032:Zinc; D002118:Calcium