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Novel natural peptides from Hyla arborea schelkownikowi skin secretion
Author(s) -
Samgina T. Yu.,
Gorshkov V.A.,
Artemenko K.A.,
Kovalev S.V.,
Ogourtsov S.V.,
Zubarev R. A,
Lebedev A.T.
Publication year - 2010
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.4571
Subject(s) - chemistry , dissociation (chemistry) , electrospray ionization , acetylation , mass spectrometry , peptide , fragmentation (computing) , secretion , fourier transform ion cyclotron resonance , electron transfer dissociation , chromatography , stereochemistry , biochemistry , tandem mass spectrometry , organic chemistry , ecology , gene , biology
Hyla arborea schelkownikowi is one of the leaf frog species inhabiting the southern territories of Russia and the former USSR. This frog species is a member of the Hylidae Rafinesque, 1815 batrachians family. The present study deals with the previously uninvestigated peptidome of the Hyla arborea schelkownikowi skin secretion. Nano‐electrospray ionization Fourier transform mass spectrometry (nanoESI‐FTMS) of the skin secretion, in the intact form and after acetylation, was selected as the general method of analysis. Electron‐capture dissociation (ECD) and collision‐induced dissociation (CID) fragmentation were both employed, while de novo sequencing was performed by manual interpretation of the MS data. The suppression of the cyclization of b‐ ions in the mass spectrometer by the acetylation reaction proved to be very efficient for the de novo sequencing of short peptides. Ten skin peptides were found and all of them, except for bradykinin, had not previously been reported. Six of the peptides belong to the tryptophyllins and related peptides, while three peptides are similar to the aureins. Copyright © 2010 John Wiley & Sons, Ltd.