Premium
Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii : sequence determination by electrospray mass spectrometry
Author(s) -
Wegener Kate L.,
Brinkworth Craig S.,
Bowie John H.,
Wallace John C.,
Tyler Michael J.
Publication year - 2001
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.429
Subject(s) - chemistry , electrospray mass spectrometry , edman degradation , mass spectrometry , electrospray , frog skin , antimicrobial , chromatography , biochemistry , peptide sequence , organic chemistry , sodium , gene
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). Copyright © 2001 John Wiley & Sons, Ltd.