HIV-1 Inhibiting Capacity of Novel Forms of Presentation of GB Virus C Peptide Domains is Enhanced by Coordination to Gold Compounds

Author(s): María J. Gómara, Ramona Galatola, Alejandro Gutiérrez, María C. Gimeno, José M. Gatell, Víctor Sánchez-Merino, Eloísa Yuste, Isabel Haro

Journal Name: Current Medicinal Chemistry

Volume 21 , Issue 2 , 2014

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Following the report of beneficial effects of co-infection by GB virus C (GBV-C) for HIV-infected patients, we have studied synthetic GBV-C peptides and their relationship with HIV type-1. This paper reports the design and synthesis of new forms of presentation of two peptide inhibitors corresponding to the envelope proteins E1 and E2 of GBV-C, together with a study of their anti-HIV-1 activity. Homogeneous and heterogeneous multiple antigenic peptides (MAPs), lipophilic derivatizations, cyclization and peptide–gold conjugations are the chemical design strategies adopted. Our aim is to enhance the anti-viral potency of the GBV-C peptide domains. Of all the GBV-C peptide derivatives studied, peptide–gold complexes derived from the (22-39) sequence of the GBV-C E1 protein were the most active entry inhibitors. These results support the putative modulation of HIV-1 infection by the GBV-C E1 protein and open new perspectives for the development of novel peptide-derived HIV-1 entry inhibitors.

Keywords: Anti-HIV assays, cell–cell fusion assays, cyclic peptides, GBV-C, HIV-1, lipopeptides, multiple antigenic peptides, peptide–gold complexes.

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Article Details

Year: 2014
Published on: 06 December, 2013
Page: [238 - 250]
Pages: 13
DOI: 10.2174/09298673113206660276
Price: $65

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