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Differences in secondary structure of HAV‐synthetic peptides induced by the sequential order of T‐ and B‐cell epitopes
Author(s) -
Gómara M. J.,
Girona V.,
Ercilla G.,
Reig F.,
Alsina M. A.,
Haro I.
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(200102)58:2<117::aid-bip10>3.0.co;2-4
Subject(s) - random coil , epitope , chemistry , peptide , deconvolution , sequence (biology) , fluorescence , computational biology , protein secondary structure , biophysics , biological system , combinatorial chemistry , biochemistry , algorithm , antibody , immunology , computer science , physics , quantum mechanics , biology
The present study was undertaken to examine the structural features of two peptide constructs designed on the basis of linear combination of B and T‐cell epitopes in different orientations (BT and TB) that may be important to explain the differences in the elicited antihepatitis A virus immune response and in the interaction with biological model membranes. A CD study was carried out and the corresponding quantitative analysis of the experimental data was done using deconvolution computer programs. Moreover, fluorescence experiments were performed to analyze differences in the fluorescence emission spectra of both molecules. The main conformational difference by CD studies was obtained working in aqueous medium. Although the TB sequence adopted a preferably random coil structure, the BT peptide was best fitted with β‐type structures. These results are further supported by fluorescence studies. These findings have relevance for the design of synthetic immunopeptides. © 2001 John Wiley & Sons, Inc. Biopoly 58: 117–128, 2001