Lipid-induced changes in the secondary structure of snake venom cardiotoxins

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DOIResolve DOI: https://doi.org/10.1016/S0021-9258(19)35423-7
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  1. National Research Council of Canada
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Abstract
The secondary structures of three snake venom cardiotoxins (from Hemachatus hemachatus, Naja naja atra, and Naja naja naja), in aqueous solution and in a lipid-bound form, were investigated by Fourier-transform infrared spectroscopy. The conformation-sensitive protein infrared bands in the amide I region were analyzed using deconvolution and band-fitting procedures. The spectra of the three cardiotoxins in aqueous buffer are very similar; they indicate a high content of both antiparallel beta-sheet structure and unordered conformation. Moreover, component bands characteristic of turns can also be identified. The binding of cardiotoxins to bilayers of dimyristoylphosphatidyl-glycerol results in an increased content of a beta-structure at the expense of the nonordered conformation. It is suggested that lipid-induced conformational transitions to a beta-structure, similar to that observed with cardiotoxins, may be operative also in membrane interaction of other proteins and peptides, particularly with those which have a small tendency to form alpha-helices.
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PublisherThe American Society for Biochemistry and Molecular Biology
Elsevier
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  • The Journal of Biological Chemistry 263, no. 2 (15 January 1988): 786–790.
LanguageEnglish
Peer reviewedYes
NPARC number23001353
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