Call for Papers  

Article Details


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

[ Vol. 21 , Issue. 2 ]

Author(s):

María J. Gómara, Ramona Galatola, Alejandro Gutiérrez, María C. Gimeno, José M. Gatell, Víctor Sánchez-Merino, Eloísa Yuste and Isabel Haro   Pages 238 - 250 ( 13 )

Abstract:


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.

Affiliation:

, , , , , , , Unit of Synthesis and Biomedical Applications of Peptides, IQAC-CSIC, Spain.



Read Full-Text article