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Molecules 2017, 22(12), 2199; https://doi.org/10.3390/molecules22122199

Conserved Binding Regions Provide the Clue for Peptide-Based Vaccine Development: A Chemical Perspective

1
Colombian Institute of Immunology Foundation (FIDIC Nonprofit-Making Organisation), Bogotá 111321, Colombia
2
School of Medicine and Health Sciences, University of Rosario, Bogotá 111321, Colombia
3
Faculty of Health Sciences, Applied and Environmental Sciences University (UDCA), Bogotá 111321, Colombia
4
Faculty of Medicine, National University of Colombia, Bogotá 111321, Colombia
*
Author to whom correspondence should be addressed.
Received: 27 October 2017 / Revised: 24 November 2017 / Accepted: 27 November 2017 / Published: 12 December 2017
(This article belongs to the Special Issue Peptide Therapeutics)
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Abstract

Synthetic peptides have become invaluable biomedical research and medicinal chemistry tools for studying functional roles, i.e., binding or proteolytic activity, naturally-occurring regions’ immunogenicity in proteins and developing therapeutic agents and vaccines. Synthetic peptides can mimic protein sites; their structure and function can be easily modulated by specific amino acid replacement. They have major advantages, i.e., they are cheap, easily-produced and chemically stable, lack infectious and secondary adverse reactions and can induce immune responses via T- and B-cell epitopes. Our group has previously shown that using synthetic peptides and adopting a functional approach has led to identifying Plasmodium falciparum conserved regions binding to host cells. Conserved high activity binding peptides’ (cHABPs) physicochemical, structural and immunological characteristics have been taken into account for properly modifying and converting them into highly immunogenic, protection-inducing peptides (mHABPs) in the experimental Aotus monkey model. This article describes stereo–electron and topochemical characteristics regarding major histocompatibility complex (MHC)-mHABP-T-cell receptor (TCR) complex formation. Some mHABPs in this complex inducing long-lasting, protective immunity have been named immune protection-inducing protein structures (IMPIPS), forming the subunit components in chemically synthesized vaccines. This manuscript summarizes this particular field and adds our recent findings concerning intramolecular interactions (H-bonds or π-interactions) enabling proper IMPIPS structure as well as the peripheral flanking residues (PFR) to stabilize the MHCII-IMPIPS-TCR interaction, aimed at inducing long-lasting, protective immunological memory. View Full-Text
Keywords: synthetic peptides; therapeutics; immunogenicity; malaria vaccine; structure synthetic peptides; therapeutics; immunogenicity; malaria vaccine; structure
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Curtidor, H.; Reyes, C.; Bermúdez, A.; Vanegas, M.; Varela, Y.; Patarroyo, M.E. Conserved Binding Regions Provide the Clue for Peptide-Based Vaccine Development: A Chemical Perspective. Molecules 2017, 22, 2199.

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