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.
journal_name
Vaccinejournal_title
Vaccineauthors
Bermúdez A,Calderon D,Moreno-Vranich A,Almonacid H,Patarroyo MA,Poloche A,Patarroyo MEdoi
10.1016/j.vaccine.2014.02.003subject
Has Abstractpub_date
2014-04-11 00:00:00pages
2117-26issue
18eissn
0264-410Xissn
1873-2518pii
S0264-410X(14)00175-3journal_volume
32pub_type
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