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Article

Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.

ACS chemical biology - 18 Dec 2015

Bailey Lauren D, Kalyana Sundaram Ramalingam Venkat, Li Huiyuan, Duffy Caitlin, Aneja Rachna, Rosemary Bastian Arangassery, Holmes Andrew P, Kamanna Kantharaju, Rashad Adel A, Chaiken Irwin

Abstract excerpt

We investigated the mode of action underlying lytic inactivation of HIV-1 virions by peptide triazole thiol (PTT), in particular the relationship between gp120 disulfides and the C-terminal cysteine-SH required for virolysis. Obligate PTT dimer obtained by PTT SH cross-linking and PTTs with serially truncated linkers between pharmacophore isoleucine-ferrocenyltriazole-proline-tryptophan and cysteine-SH were...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26458166
DOI: 10.1021/acschembio.5b00381
PMCID: PMC4836388

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