Journal
EUROPEAN JOURNAL OF MASS SPECTROMETRY
Volume 17, Issue 1, Pages 73-83Publisher
IM PUBLICATIONS
DOI: 10.1255/ejms.1110
Keywords
MALDI; post-source decay; Rana ridibunda; cystine-containing amphibian peptides; de novo sequencing; maleimide; on-plate reduction
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Long disulfide-containing peptides, brevinins 1E and 2Ec, from the skin secretion of the frog Rana ridibunda were reduced and alkylated with ten novel and three known derivatizing agents. Nine of novel reagents are maleimide derivatives. The peptides were also reduced with dithiothreitol directly on a matrix-assisted laser desorption/ionization MALDI) target without alkylation. Modified samples were subjected to a MALDI-post-source decay study. Procedures, fragmentation patterns, fragment ion signal abundances and sequence coverage for two peptides modified with 13 tags (or on-plate reduced) are described. The fast on-plate procedure for reduction/alkylation was applied to a crude secretion from Rana ridibunda, providing intense signals of derivatized peptides. The corresponding ions may be used for the tandem mass spectrometry sequencing procedure.
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