The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata
Date
2003
Authors
Brinkworth, C.
Carver, J.
Wegener, K.
Doyle, J.
Llewellyn, L.
Bowie, J.
Editors
Advisors
Journal Title
Journal ISSN
Volume Title
Type:
Journal article
Citation
Biopolymers, 2003; 70(3):424-434
Statement of Responsibility
Craig S. Brinkworth, John A. Carver, Kate L. Wegener, Jason Doyle, Lyndon E. Llewellyn and John H. Bowie
Conference Name
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.
School/Discipline
Dissertation Note
Provenance
Published Online: 2 Oct 2003
Description
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