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Type: Journal article
Title: The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata
Author: Brinkworth, C.
Carver, J.
Wegener, K.
Doyle, J.
Llewellyn, L.
Bowie, J.
Citation: Biopolymers, 2003; 70(3):424-434
Publisher: John Wiley & Sons Inc
Issue Date: 2003
ISSN: 0006-3525
Statement of
Craig S. Brinkworth, John A. Carver, Kate L. Wegener, Jason Doyle, Lyndon E. Llewellyn and John H. Bowie
Abstract: The peptide frenatin 3 is a major component of the skin secretion of the Australian giant tree frog, Litoria infrafrenata. Frenatin 3 is 22 amino acids in length, and shows neither antimicrobial nor anticancer activity. It inhibits the production of nitric oxide by the enzyme neuronal nitric oxide synthase at a micromolar concentration by binding to its regulatory protein, Ca2+ calmodulin, a protein known to recognize and bind amphipathic alpha-helices. The solution structure of frenatin 3 has been investigated using NMR spectroscopy and restrained molecular dynamics calculations. In trifluoroethanol/water mixtures, the peptide forms an amphipathic alpha-helix over residues 1-14 while the C-terminal eight residues are more flexible and less structured. The flexible region may be responsible for the lack of antimicrobial activity. In water, frenatin 3 exhibits some alpha-helical character in its N-terminal region.
Keywords: amphibian peptides
neuronal nitric oxide synthase inhibition
NMR spectroscopy
solution structure
Description: The definitive version may be found at
Provenance: Published Online: 2 Oct 2003
DOI: 10.1002/bip.10524
Published version:
Appears in Collections:Aurora harvest
Chemistry publications

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