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Type: Journal article
Title: Host-defence skin peptides of the Australian Streambank Froglet Crinia riparia: isolation and sequence determination by positive and negative ion electrospray mass spectrometry
Author: Maselli, V.
Bilusich, D.
Bowie, J.
Tyler, M.
Citation: Rapid Communications in Mass Spectrometry, 2006; 20(5):797-803
Publisher: John Wiley & Sons Ltd
Issue Date: 2006
ISSN: 0951-4198
Statement of
Vita M. Maselli, Daniel Bilusich, John H. Bowie, Michael J. Tyler
Abstract: A combination of positive and negative ion electrospray mass spectrometry (ES-MS) together with automated Edman sequencing has been used to determine the amino acid sequences of the host-defence peptides from the skin glands of the froglet Crinia riparia. The peptides are called riparins. Of the eight peptides isolated, five are neuropeptides containing intramolecular disulfide linkages; e.g. the major peptide riparin 1.4 (FFLPPCAYKGTC-OH). Positive ion ES-MS identifies the five residues of riparin 1.4 outside the disulfide moiety, but provides no information on the sequence within the disulfide ring. In contrast, the negative ion dissociations of the [M-H]- ion of riparin 1.4 identify the --S-S-- link by loss of H2S2 from the [M-H]- ion, and also provide the sequence within the disulfide unit. Other peptides are riparin 2.1 [(IIEKLVNTALGLLSGL-NH2), a narrow-spectrum antibiotic], signiferin 3.1 [(GIAEFLNYIKSKA-NH2), an nNOS inhibitor] and riparin 5.1 [IVSYPDDAGEHAHKMG-NH2], which shows no neuropeptide, antibiotic or nNOS activity.
Keywords: Skin
Chromatography, High Pressure Liquid
Spectrometry, Mass, Electrospray Ionization
Sequence Analysis, Protein
Amino Acid Sequence
Molecular Sequence Data
Description: The definitive version may be found at
DOI: 10.1002/rcm.2360
Appears in Collections:Aurora harvest 2
Chemistry publications

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