Gauche+ side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine
作者： Adriana Bermúdez , Dayana Calderon , Armando Moreno-Vranich , Hannia Almonacid , Manuel A Patarroyo
DOI: 10.1016/J.VACCINE.2014.02.003
关键词: Peptide binding 、 Binding site 、 Protein structure 、 Protein subunit 、 Stereochemistry 、 Peptide sequence 、 Biology 、 Virology 、 Polyproline helix 、 Amino acid 、 Peptide vaccine 、 Public Health, Environmental and Occupational Health 、 General Immunology and Microbiology 、 Molecular medicine 、 General Veterinary 、 Infectious Diseases
摘要: 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 complete full protection antimalarial vaccine development producing a large panel of individually fully protection-inducing protein structures (FPIPS) very long-lasting antibody-inducing (VHLLAI) mHABPs. Most those which did not interfere, compete, inhibit or suppress their individual VHLLAI FPIPS contained displayed polyproline II-like (PPIIL) structure when mixed. Here we show that amino acid side-chains located peptide region (PBR) positions p3 p7 specific electron charges side-chain gauche+ orientation interacting with the TCR. Based on above, previously described physicochemical principles, non-interfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically mHABP mixtures can be designed developing vaccines against diseases scourging humankind, malaria being one them.
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