Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry

K L Wegener; C S Brinkworth; J H Bowie; J C Wallace; M J Tyler

doi:10.1002/rcm.429

Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry

Rapid Commun Mass Spectrom. 2001;15(18):1726-34. doi: 10.1002/rcm.429.

Authors

K L Wegener¹, C S Brinkworth, J H Bowie, J C Wallace, M J Tyler

Affiliation

¹ Department of Chemistry, The University of Adelaide, South Australia, 5005.

PMID: 11555873
DOI: 10.1002/rcm.429

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).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Bufonidae / metabolism*
Chromatography, High Pressure Liquid
Hydrolysis
Molecular Sequence Data
Oligopeptides / chemistry*
Spectrometry, Mass, Electrospray Ionization

Substances

Oligopeptides
dahlein peptides