Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/4850
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Type: Journal article
Title: Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry
Author: Wegener, K.
Brinkworth, C.
Bowie, J.
Wallace, J.
Tyler, M.
Citation: Rapid Communications in Mass Spectrometry, 2001; 15(18):1726-1734
Publisher: John Wiley & Sons Ltd
Issue Date: 2001
ISSN: 0951-4198
1097-0231
Statement of
Responsibility: 
Kate L. Wegener, Craig S. Brinkworth, John H. Bowie, John C. Wallace, Michael J. Tyler
Abstract: Eleven dahlein peptides are present in the skin secretion of the Australian aquatic frog Litoria dahlii. All peptides have been sequenced using a combination of electrospray mass spectrometry (ES-MS) and Lys-C digestion/MS, with each sequence confirmed by automated Edman sequencing. The 13-residue dahlein 1 peptides (e.g. dahlein 1.1 GLFDIIKNIVSTL-NH(2)) exhibit weak wide-spectrum antimicrobial activity but no significant activity in the anticancer testing program of the National Cancer Institute (Washington). There are no potent antimicrobial peptides present in the glandular secretion, but the dahleins 5 strongly inhibit the formation of NO by neuronal nitric oxide synthase (e.g. dahlein 5.1 GLLGSIGNAIGAFIANKLKP-OH).
Keywords: Animals
Bufonidae
Oligopeptides
Chromatography, High Pressure Liquid
Spectrometry, Mass, Electrospray Ionization
Amino Acid Sequence
Hydrolysis
Molecular Sequence Data
Description: The definitive version may be found at www.wiley.com
DOI: 10.1002/rcm.429.abs
Published version: http://www3.interscience.wiley.com/cgi-bin/fulltext/85010855/PDFSTART
Appears in Collections:Aurora harvest 6
Chemistry publications

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