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Cyclic Peptidomimetics Derived from the Apical Membrane Antigen I of Plasmodium falciparum and Their Use in Malaria Vaccine Design
Author(s) -
Renard Annabelle,
Mueller Markus,
Zurbriggen Rinaldo,
Pluschke Gerd,
Robinson John A.
Publication year - 2003
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.200390309
Subject(s) - peptidomimetic , chemistry , dipeptide , antigen , epitope , plasmodium falciparum , monoclonal antibody , amino acid , proline , cyclic peptide , peptide , antibody , stereochemistry , virology , biochemistry , malaria , biology , immunology
A library of 35 cyclic peptidomimetics has been prepared, by a combination of solid‐ and solution‐phase methods, which, together, scan amino acid residues 444–489 in a protruding loop in the subdomain‐III of the apical membrane antigen‐I (AMA‐I), an integral membrane protein found on the surface of Plasmodium falciparum merozoites. The mimetics each contain twelve residues from AMA‐I linked through the N‐ and C‐termini to a β ‐hairpin‐inducing template, comprising the dipeptide D ‐proline ‐ L ‐Apro (Apro= cis ‐4‐amino‐ L ‐proline). These peptidomimetics were each coupled via the 4‐amino group to a phospholipid, which allows their incorporation into reconstituted influenza virus‐like particles (virosomes) for immunization of mice, as well as their use in ELISA to characterize epitopes recognized by anti‐AMA‐I growth‐inhibitory monoclonal antibodies.