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

From National Research Council Canada

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DOIResolve DOI: https://doi.org/10.1016/S0021-9258(19)35423-7
AuthorSearch for: 1; Search for: 1; Search for: 1; Search for: 1
Name affiliation
  1. National Research Council of Canada
FormatText, Article
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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Record identifier67a5402c-b2b9-4e3d-b964-90246af114cf
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