Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine Academic Article

abstract

  • Topological and stereo-electron characteristics are essential in major histocompability class II-peptide-T-cell receptor (MHC-p-TCR) complex formation for inducing an appropriate immune response. Modified high activity binding peptides (mHABPs) were synthesised for complete full protection antimalarial vaccine development producing a large panel of individually fully protection-inducing protein structures (FPIPS) and very high long-lasting antibody-inducing (VHLLAI) mHABPs. Most of those which did not interfere, compete, inhibit or suppress their individual VHLLAI or FPIPS activity contained or displayed a polyproline II-like (PPIIL) structure when mixed. Here we show that amino acid side-chains located in peptide binding region (PBR) positions p3 and p7 displayed specific electron charges and side-chain gauche+ orientation for interacting with the TCR. Based on the above, and previously described physicochemical principles, non-interfering, long-lasting, full protection-inducing, multi-epitope, multistage, minimal subunit-based chemically synthesised mHABP mixtures can be designed for developing vaccines against diseases scourging humankind, malaria being one of them. © 2014 Elsevier Ltd.

publication date

  • 2014/4/11

edition

  • 32

keywords

  • Amino Acids
  • Antibodies
  • Antimalarials
  • Electrons
  • Epitopes
  • Malaria
  • Peptide T
  • Peptides
  • Proteins
  • T-Cell Antigen Receptor
  • T-lymphocytes
  • Vaccines
  • amino acids
  • antibodies
  • antimalarials
  • electrons
  • epitopes
  • immune response
  • malaria
  • peptides
  • polyproline
  • protein structure
  • receptors
  • vaccine development
  • vaccines

International Standard Serial Number (ISSN)

  • 0264-410X

number of pages

  • 10

start page

  • 2117

end page

  • 2126