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Synthesis of a trimeric gp120 epitope mimic conjugated to a T-helper peptide to improve antigenicity.

ABSTRACT: A fully synthetic trivalent mimotope of gp120 conjugated to pan allelic HLA DR binding epitope was prepared using solid-phase peptide synthesis and optimized copper-catalyzed azide-alkyne cycloaddition. The methodology efficiently provides chemically uniform heteromultimeric peptide constructs with enhanced binding, avidity, and specificity toward an established HIV-neutralizing human antibody, MAb b12. The versatile synthetic strategy serves as a powerful platform for the development of synthetic peptides as potential HIV-1 vaccine candidates.

SUBMITTER: Schellinger JG

PROVIDER: S-EPMC3062786 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Synthesis of a trimeric gp120 epitope mimic conjugated to a T-helper peptide to improve antigenicity.

Schellinger Joan G JG Danan-Leon Lieza M LM Hoch Jessica A JA Kassa Aemro A Srivastava Indresh I Davis David D Gervay-Hague Jacquelyn J

Journal of the American Chemical Society 20110222 10

A fully synthetic trivalent mimotope of gp120 conjugated to pan allelic HLA DR binding epitope was prepared using solid-phase peptide synthesis and optimized copper-catalyzed azide-alkyne cycloaddition. The methodology efficiently provides chemically uniform heteromultimeric peptide constructs with enhanced binding, avidity, and specificity toward an established HIV-neutralizing human antibody, MAb b12. The versatile synthetic strategy serves as a powerful platform for the development of synthet ...[more]

PMID: 21341746

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