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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]

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