Bioactive dahlein peptides from the skin secretions of the Australian aquatic frog Litoria dahlii: sequence determination by electrospray mass spectrometry.
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).
Wegener
K L
KL
Department of Chemistry, The University of Adelaide, South Australia, 5005.
Brinkworth
C S
CS
Bowie
J H
JH
Wallace
J C
JC
Tyler
M J
MJ
D000595:Amino Acid Sequence; D000818:Animals; D002025:Bufonidae / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
D009842:Oligopeptides; C437946:dahlein peptides