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Electrospray ionization mass spectrometric observation of ligand exchange of zinc pyrithione with amino acids
Author(s) -
Moriwaki Hiroshi,
Okabayashi Masanori,
Watanabe Takehiro,
Kawasaki Hideya,
Arakawa Ryuichi
Publication year - 2009
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/rcm.4128
Subject(s) - chemistry , electrospray ionization , zinc , amino acid , peptide , combinatorial chemistry , serine , mass spectrometry , electrospray , glycine , histidine , chromatography , organic chemistry , biochemistry , enzyme
Zinc pyrithione (ZnPT) is widely used as an antidandruff or antifouling reagent. However, this compound is considered toxic, such as the teratogenic effect, to aquatic lives, and it is important to clarify the mechanism of its toxicity. In this study, the interactions between ZnPT and amino acids were observed using electrospray ionization mass spectrometry (ESI‐MS) in order to obtain information on the activity of ZnPT within the living body. The ZnPT complex ([ZnPT‐ligand+Amino acid] + ), in which the ligand of ZnPT was exchanged by the amino acid, was detected in ZnPT solutions mixed with one of 20 amino acids by ESI‐MS. Histidine and cysteine, in particular, showed a high reactivity with ZnPT, while serine and glycine showed a low reactivity. The complexes of ZnPT and a peptide were also observed by the ESI‐MS measurement of the solution containing ZnPT with the peptide. These results would be useful to understand the mechanism of ZnPT toxicities to living creatures. Copyright © 2009 John Wiley & Sons, Ltd.