Differences in secondary structure of HAV-synthetic peptides induced by the sequential order of T- and B-cell epitopes

Biopolymers. 2001 Feb;58(2):117-28. doi: 10.1002/1097-0282(200102)58:2<117::AID-BIP10>3.0.CO;2-4.

Abstract

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 beta-type structures. These results are further supported by fluorescence studies. These findings have relevance for the design of synthetic immunopeptides.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / chemistry*
  • Antigens, Viral / genetics
  • B-Lymphocytes / immunology
  • Circular Dichroism
  • Epitopes / chemistry*
  • Epitopes / genetics
  • Hepatovirus / chemistry*
  • Hepatovirus / genetics
  • Hepatovirus / immunology*
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / immunology
  • Protein Structure, Secondary
  • Spectrometry, Fluorescence
  • T-Lymphocytes / immunology
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / immunology

Substances

  • Antigens, Viral
  • Epitopes
  • Peptide Fragments
  • Viral Proteins