Host‐defence skin peptides of the Australian Common Froglet  Crinia signifera : sequence determination using positive and negative ion electrospray mass spectra | Zendy

Maselli Vita M. | Zendy; Brinkworth Craig S. | Zendy; Bowie John H. | Zendy; Tyler Michael J. | Zendy

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Host‐defence skin peptides of the Australian Common Froglet Crinia signifera : sequence determination using positive and negative ion electrospray mass spectra

Author(s) -

Maselli Vita M.,

Brinkworth Craig S.,

Bowie John H.,

Tyler Michael J.

Publication year - 2004

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.1602

Subject(s) - chemistry , edman degradation , fragmentation (computing) , electrospray , ion , tandem mass spectrometry , mass spectrum , peptide , peptide sequence , chromatography , collision induced dissociation , cleavage (geology) , dissociation (chemistry) , mass spectrometry , stereochemistry , organic chemistry , biochemistry , computer science , gene , operating system , geotechnical engineering , fracture (geology) , engineering

The amino acid sequences of seven signiferin peptides are provided by consideration of tandem mass spectrometric (MS/MS) data for the respective MH + and [MH] − precursor ions. These methods do not differentiate between isomeric residues Leu and Ile; these were identified using the Edman degradation technique. The sequence of signiferin 1, a new smooth muscle contracting neuropeptide (RL CIPYIIPC ‐OH) containing a disulfide bridge, is best determined using the collision‐induced dissociation (CID) spectrum of the [MH] − anion. The initial fragmentation of this system involves loss of H 2 S 2 , which furnishes an open‐chain system that is readily sequenced using the α and β backbone cleavage anions. Copyright © 2004 John Wiley & Sons, Ltd.

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