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dc.contributor.authorPerriman, A.
dc.contributor.authorApponyi, M.
dc.contributor.authorBuntine, Mark
dc.contributor.authorJackway, R.
dc.contributor.authorRutland, M.
dc.contributor.authorWhite, J.
dc.contributor.authorBowie, J.
dc.identifier.citationPerriman, Adam W. and Apponyi, Margit A. and Buntine, Mark A. and Jackway, Rebecca J. and Rutland, Mark W. and White, John W. and Bowie, John H. 2008. Surface movement in water of splendipherin, the aquatic male sex pheromone of the tree frog Litoria splendida. FEBS Journal 275 (13): pp. 3362-3374.

The aquatic sex pheromone splendipherin (GLVSSIGKALGGLLADVVKSKGQPA-OH) of the male green tree frog Litoria splendida movesacross the surface of water to reach the female. Surface pressure and X-ray reflectometry measurements confirm that splendipherin is a surface-active molecule, and are consistent with it having an ordered structure, whereby the hydrophilic portion of the peptide interacts with the underlying water and the hydrophobic region is adjacent to the vapour phase. The movementof splendipherin over the surface of water is caused by a surface pressure gradient. In order to better define the structure of splendipherin at the water / air interface we used 2D NMR studies of the pheromone with the solvent system trifluoroethanol / water (1 : 1 v/v). In this solvent system,splendipherin adopts a bent a helix from residues V3 to K21. The bending of the helix occurs in the centre of the peptide in the vicinity of G11 and G12. The region of splendipherin from V3 to G11 has well-defined amphipathicity, whereas the amphipathicity from G12 to A25 is reduced by K19and P24 intruding into the hydrophobic and hydrophilic regions respectively. A helical structure is consistent with X-ray reflectometry data.

dc.publisherBlackwell Publishing
dc.subject2D NMR
dc.subjectX-ray reflectometry
dc.subjectsurface pressure gradient
dc.subjectsex pheromone
dc.titleSurface movement in water of splendipherin, the aquatic male sex pheromone of the tree frog Litoria splendida
dc.typeJournal Article
dcterms.source.titleFEBS Journal
curtin.accessStatusOpen access via publisher

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