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|Title:||The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata|
|Citation:||Biopolymers, 2003; 70(3):424-434|
|Publisher:||John Wiley & Sons Inc|
|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|
|Appears in Collections:||Chemistry publications|
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