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Complexes between some lysine‐containing peptides and crown ethers—electrospray ionization mass spectrometric study
Author(s) -
Frański Rafał,
Schroeder Grzegorz,
Kamysz Wojciech,
Niedzialkowski Pawel,
Ossowski Tadeusz
Publication year - 2007
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1178
Subject(s) - chemistry , electrospray ionization , chromatography , mass spectrometry , electrospray , lysine , extractive electrospray ionization , protein mass spectrometry , amino acid , biochemistry
The complexes between lysine‐containing peptides (M) and crown ethers (CEs, 18C6, 15C5, 12C4) have been studied by the electrospray ionization (ESI) mass spectrometry. The maximum number of CEs attached has been found to be the same as that of the alkyl‐amino side chains of lysine and as that of the protons attached. Examination of the breakdown plots of the abundances of the ions observed against the cone voltage (CV) has shown that mass spectrometric fragmentation pathways of [M + nH + (CE) n ] + n may involve a loss of a neutral CE molecule as well as protonated one. The decrease in the CE cavity (the use of 12C4 or 15C5 instead of 18C6) leads to a dramatic lowering in the stability of the complexes in the gas phase but not in solution. Attachment of a CE to peptides increases their hydrophobicity, and therefore proceeds with lower efficiency in water than in methanol. Copyright © 2007 John Wiley & Sons, Ltd.