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Evaluation of the metal binding properties of the histidine‐rich antimicrobial peptides histatin 3 and 5 by electrospray ionization mass spectrometry
Author(s) -
Brewer Dyanne,
Lajoie Gilles
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001015)14:19<1736::aid-rcm86>3.0.co;2-2
Subject(s) - chemistry , electrospray ionization , circular dichroism , mass spectrometry , metal , peptide , histidine , metal ions in aqueous solution , electrospray , ion , crystallography , chromatography , organic chemistry , biochemistry , enzyme
Electrospray ionization mass spectrometry (ESI‐MS) was used to investigate metal ion interactions with salivary peptides histatin 3 (H3) and histatin 5 (H5). Conformational changes of these peptides in the presence of metal ions were studied using circular dichroism spectroscopy. H3 and H5 formed high affinity complexes with Cu 2+ and Ni 2+ and, to a lesser extent, with Zn 2+ . Both peptides show the potential for multiple binding sites for Cu 2+ and Ni 2+ and only a single strong binding site for Zn 2+ . The binding of a third Cu 2+ ion to H3 seems to enable the binding of a fourth ion to H3. The binding of a second and third Ni 2+ ion to H5 has a similar effect in enabling the binding of a fourth ion. None of the metal ions examined stabilized a regular secondary structure for either peptide. Subtle changes in overall conformation are seen with the addition of Cu 2+ to both H3 and H5. Copyright © 2000 John Wiley & Sons, Ltd.