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https://hdl.handle.net/2440/39363
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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 1097-0282 |
Statement of Responsibility: | 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 www.wiley.com |
Provenance: | Published Online: 2 Oct 2003 |
DOI: | 10.1002/bip.10524 |
Published version: | http://www3.interscience.wiley.com/journal/105561429/abstract |
Appears in Collections: | Aurora harvest Chemistry publications |
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