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Type: Journal article
Title: Negative ion electrospray mass spectra of the maculatin peptides from the tree frogs Litoria genimaculata and Litoria eucnemis
Author: Brinkworth, C.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2003; 17(19):2215-2225
Publisher: John Wiley & Sons Ltd
Issue Date: 2003
ISSN: 0951-4198
Statement of
Craig S. Brinkworth, John H. Bowie
Abstract: Collision-induced fragmentations of deprotonated maculatin 1 peptides provide significant sequencing information. When the peptide lacks those residues which can fragment through their alpha side chains (e.g. Thr, Ser, Glu and Gln in this study) the basic alpha and beta' backbone cleavages occur from the [Mbond;H](-) anion. When Thr, Ser, Glu and Gln are present, the ease of side-chain fragmentation of these residues is: Thr (loss of MeCHO) > Ser (CH(2)O) > Glu (H(2)O) > Gln (NH(3)). When one of more of these residues is (are) present, the alpha and beta' cleavages often occur from a fragment rather than the [Mbond;H](-) anion, e.g. for Thr, the [(Mbond;H)(-)bond;MeCHO](-) anion. These four residues also initiate gamma backbone cleavage reactions. The relative abundances of peaks resulting from gamma cleavage are Glu > Ser = Thr > Gln for maculatin 1 spectra. An unusual Gln19/Ile17 cyclisation/cleavage reaction occurs in maculatin spectra: the peptide [Mbond;H](-) anion must adopt a helical conformation in order for these two groups to interact. Analogous fragmentations have been reported previously in the negative ion spectra of the caerin 1 peptides.
Keywords: Animals
Antimicrobial Cationic Peptides
Amphibian Proteins
Spectrometry, Mass, Electrospray Ionization
Amino Acid Sequence
Protein Structure, Secondary
Models, Molecular
Computer Simulation
Molecular Sequence Data
Description: The definitive version may be found at
Provenance: Published Online: 29 Aug 2003
DOI: 10.1002/rcm.1172
Published version:
Appears in Collections:Aurora harvest 6
Chemistry publications

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