Secondary structure changes of diphtheria toxin interacting with asolectin liposomes: an infrared spectroscopy study

Biochimie
V CabiauxJ M Ruysschaert

Abstract

Until now, the study of the secondary structure of diphtheria toxin (DT) in the presence of phospholipid vesicles as a function of the pH has been prevented by the optical turbidity of the solution. In the present paper, this problem has been overcome by the use of IR attenuated total reflection (IR-ATR) spectroscopy. Incubation of DT with asolectin liposomes at pH 7.3 results in the binding of DT on to the liposomes and in a 10% increase in its alpha-helix content. At pH 4, in the presence of asolectin liposomes, the secondary structure of DT is characterized by the appearance of a beta-sheet structure with strengthened hydrogen bonds, which did not exist before lowering of the pH. This new type of beta-sheet (low frequency beta-sheet) involves 25% of the amino acid residues of the protein.

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Citations

Nov 6, 1989·Biochimica Et Biophysica Acta·E GoormaghtighJ M Ruysschaert
Jan 1, 1993·Progress in Biophysics and Molecular Biology·J L ArrondoF M Goñi
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Mar 9, 2004·Biochimica Et Biophysica Acta·Christian WolffVéronique Cabiaux
Jul 10, 2002·The Journal of Peptide Research : Official Journal of the American Peptide Society·F GaoH Wu

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