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Title: A CD STRATEGY FOR THE STUDY OF POLYPEPTIDE FOLDING-UNFOLDING (06/09/91)

Author
item SILIGARD, G - UNIVERSITY OF LONDON
item DRAKE, A - UNIVERSITY OF LONDON
item MASCAGNI, P - UNIVERSITY OF LONDON
item ROWLANDS, D - LONDON ENGLAND
item BROWN, FRED - YALE UNIVERSITY
item GIBBONS, W - UNIVERSITY OF LONDON

Submitted to: International Journal of Peptide and Protein Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/9/1991
Publication Date: N/A
Citation: N/A

Interpretive Summary: Physico-chemical methods have been used to analyse the shape of that part of foot-and-mouth disease virus that confers protection against the disease. This analysis allows predictions to be made about the best shape to confer protection against different isolates of the virus.

Technical Abstract: The circular dichroism spectrum of the 20-residue immunogenic peptide from the foot-and-mouth disease virus was solvent- and temperature- dependent. Careful solvent titration revealed two isodichroic points and plateaux consistent with stepwise unfolding of specific stable conformations. Variable temperature studies in cryogenic solvents and urea perturbation were consistent with the existence of three conformational moieties, the left-handed extended helix, the x-helix. and the 3[10] helix. The number of residues in each helix was confirmed by CD spectral simulations. The strategy described here can be used to determine the components of a conformational equilibrium and their statistical weights, to study peptide folding and unfolding and to determine the bioactive conformations(s) of linear peptides. The conclusions were supported by 2D-DMR studies. A new mechanism for the stabilization of left-handed extended helices and destabilization of x-helices by urea is proposed. The structure of the peptide as resolved by CD spectroscopy is of particular significance since the conformation of this antigenic sequence in situ has so far not been solved by X-ray crystallography.