The conformational restriction of synthetic peptides, including a malaria peptide, for use as immunogens.

A. C. Satterthwait, T. Arrhenius, R. A. Hagopian, F. Zavala, V. Nussenzweig, R. A. Lerner

Research output: Contribution to journalArticlepeer-review

Abstract

A new strategy is advanced for the conformational restriction of peptidyl immunogens. Our approach is to replace putative amide-amide hydrogen bonds with covalent hydrogen-bond mimics. Because on average every other amino acid in a protein engages in this bond, the syntheses of diversely shaped peptides can be contemplated. Synthetic methods for introducing a potential hydrogen-bond mimic into a peptide with alpha-helical potential is reported and the structural consequences are discussed. The replacement of the hydrogen bond with a chemical link will modify as well as shape the peptide. To explore the consequences of these changes, a potential synthetic vaccine for malaria, the repeating tetrapeptide Asn-Pro-Asn-Ala, was conformationally restricted. Antibodies to the shaped malarial peptide showed a strong cross reaction with Plasmodium falciparum sporozoites.

Original languageEnglish (US)
Pages (from-to)565-572
Number of pages8
JournalPhilosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume323
Issue number1217
DOIs
StatePublished - Jun 12 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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