Buré Corinne, Maget Régine, Delmas Agnès F, Pichon Chantal, Midoux Patrick
Centre de Biophysique Moléculaire CNRS UPR4301 affiliated to the University of Orléans and Inserm, Orléans cedex 2, France.
J Mass Spectrom. 2009 Jan;44(1):81-9. doi: 10.1002/jms.1473.
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, H5WYG + Zn + H and H5WYG + Zn 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.
富含组氨酸的肽H5WYG（GLFHAIAHFIHGGWHGLIHGWYG）被发现在生理pH值且存在氯化锌的情况下可诱导膜融合。在本研究中，我们检测了Zn(2+)与H5WYG相互作用的离子选择性。该研究通过空气/水界面吸附和质谱法进行。我们发现与Zn(2+)离子形成了肽 - 金属复合物。电喷雾电离质谱（ESI-MS）显示，随着Zn(2+)当量的增加而出现的H5WYG + Zn + 2H、H5WYG + Zn + H和H5WYG + Zn离子对应于单分子H5WYG - Zn(2+)复合物。串联质谱（MS/MS）为单个Zn(2+)离子与H(11)、H(19)以及可能的H(15)残基的结合提供了证据。
