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Front Cover: Nonaqueous capillary electrophoresis mass spectrometry method for determining highly hydrophobic peptides
Author(s) -
Cheng Jianhui,
Chen David D. Y.
Publication year - 2018
Publication title -
electrophoresis
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201870071
Subject(s) - capillary electrophoresis , chromatography , chemistry , capillary electrophoresis–mass spectrometry , mass spectrometry , analyte , aqueous solution , front cover , electrophoresis , capillary action , cover (algebra) , electrospray ionization , materials science , organic chemistry , mechanical engineering , engineering , composite material
DOI: 10.1002/elps.201700364 The cover picture shows that temporin peptides originally derived from Rana temporaria can be analysed by a well‐developed non‐aqueous capillary electrophoresis–mass spectrometry (NACE–MS) method. The structure of Temporin A, one of the analytes, is shown in this picture. The structure shows that most of the side chains in this sequence are hydrophobic. Temporins' high hydrophobicity makes it difficult to analyse it using traditional aqueous capillary electrophoresis. In this study, it is shown that NACE is capable of dealing with hydrophobic analytes.