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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide.

The conformational properties of the atrial natriuretic peptide atriopeptin III were investigated by Fourier-transform infrared spectroscopy. Infrared spectra in the amide I region were analyzed quantitatively using deconvolution and band-fitting procedures. According to this analysis, in aqueous solution the monomeric peptide has a random structure. Binding to bilayer vesicles of dimyristoyl phosphatidylglycerol results in drastic conformational changes. The lipid-complexed atriopeptin III adopts a highly ordered structure of predominantly beta-sheets. A transition to a similar, but not identical, beta-structure occurs upon self-association of the peptide. The results of model experiments suggest that the binding of this atrial peptide to the target cell membrane is associated with the induction of beta-sheet structure and that it is this latter conformation that is predominant in the active form of the hormone.[1]


  1. Infrared spectroscopic evidence of conformational transitions of an atrial natriuretic peptide. Surewicz, W.K., Mantsch, H.H., Stahl, G.L., Epand, R.M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
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