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The conformational restriction of synthetic vaccines for malaria

Academic Article
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Overview

authors

  • Satterthwait, A. C.
  • Chiang, L. C.
  • Arrhenius, T.
  • Cabezas, E.
  • Zavala, F.
  • Dyson, Jane
  • Wright, Peter
  • Lerner, Richard

publication date

  • 1990

journal

  • Bulletin of the World Health Organization  Journal

abstract

  • The effectiveness of synthetic vaccines is dependent upon the chance event that antibodies formed against largely disordered peptides can bind native protein surfaces which are often ordered. To improve on this situation, new methods are being developed for the conformational restriction of synthetic peptides. Cognate peptide sequences often form predictable secondary structures in proteins characterized by distinct hydrogen-bonding patterns. These weak hydrogen bonds have now been replaced with covalent mimics to conformationally restrict selected peptides to the Type 1 reverse turn and alpha helix. Potential uses for this chemistry are discussed in the context of malaria vaccines. The peptide component of a Plasmodium falciparum sporozoite vaccine, acetyl-(ASN-ALA-ASN-PRO)3-NH2 has been conformationally analysed using two-dimensional nuclear magnetic resonance spectroscopy. These studies are consistent with the formation of transiently ordered turnlike structures which provide a guide for the design and synthesis of a conformationally restricted synthetic vaccine. To assess the effects of conformational restriction and chemical modification on the sporozoite vaccine, ASN side-chains were linked around proline with ethylene bridges. Polyclonal antibodies to this shaped peptide show a strong cross-reaction with living sporozoites.

subject areas

  • Animals
  • Drug Design
  • Hydrogen Bonding
  • Magnetic Resonance Imaging
  • Malaria
  • Plasmodium falciparum
  • Protein Conformation
  • Vaccines, Synthetic
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Identity

PubMed Central ID

  • PMC2393045

International Standard Serial Number (ISSN)

  • 0042-9686

PubMed ID

  • 2094582
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Additional Document Info

start page

  • 17

end page

  • 25

volume

  • 68

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