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Caerulein‐like peptides from the skin glands of the Australian Blue Mountains tree frog Litoria citropa . Part 1. Sequence determination using electrospray mass spectrometry
Author(s) -
Wabnitz Paul A.,
Bowie John H.,
Tyler Michael J.
Publication year - 1999
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/(sici)1097-0231(19991230)13:24<2498::aid-rcm817>3.0.co;2-e
Subject(s) - chemistry , electrospray mass spectrometry , chromatography , electrospray , mass spectrometry , sequence (biology) , biochemistry
Sixteen caerulein‐type peptides have been isolated from the skin secretions of the Australian Blue Mountains tree frog Litoria citropa . There are four groups of these peptides. The first is based on the structure of the known neuropeptide caerulein [pEQDY(SO 3 )TGWMDF‐NH 2 ], now renamed caerulein 1.1. Examples of peptides of the other groups are as follows: caerulein 2.1 [pEQDY(SO 3 )TGAHMDF‐NH 2 ], caerulein 3.1 [pEQDY(SO 3 )GTGWMDF‐NH 2 ] and caerulein 4.1 [pEQDY(SO 3 )TGSHMDF‐NH 2 ]. All of these peptides are accompanied by the associated peptide where Phe replaces Met, and all eight of the caerulein peptides are accompanied by the desulfated analogues. Negative ion electrospray mass spectrometry (ES‐MS) is used to determine the molecular weights of the caeruleins 1–4 [from their [M − H] ‐ ions], while the sequences of the peptides are determined from the B and Y + 2 cleavage ions in the mass spectra of the [MH + − SO 3 ] + ions. © 1999 John Wiley & Sons, Ltd.