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Characterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNA.

ABSTRACT: A branched peptide containing multiple boronic acids was found to bind RRE IIB selectively and inhibit HIV-1 p24 capsid production in a dose-dependent manner. Structure-activity relationship studies revealed that branching in the peptide is crucial for the low micromolar binding towards RRE IIB, and the peptide demonstrates selectivity towards RRE IIB in the presence of tRNA. Footprinting studies suggest a binding site on the upper stem and internal loop regions of the RNA, which induces enzymatic cleavage of the internal loops of RRE IIB upon binding.

SUBMITTER: Wynn JE

PROVIDER: S-EPMC4972714 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Characterization and in vitro activity of a branched peptide boronic acid that interacts with HIV-1 RRE RNA.

Wynn Jessica E JE Zhang Wenyu W Tebit Denis M DM Gray Laurie R LR Hammarskjold Marie-Louise ML Rekosh David D Santos Webster L WL

Bioorganic & medicinal chemistry 20160405 17

A branched peptide containing multiple boronic acids was found to bind RRE IIB selectively and inhibit HIV-1 p24 capsid production in a dose-dependent manner. Structure-activity relationship studies revealed that branching in the peptide is crucial for the low micromolar binding towards RRE IIB, and the peptide demonstrates selectivity towards RRE IIB in the presence of tRNA. Footprinting studies suggest a binding site on the upper stem and internal loop regions of the RNA, which induces enzymat ...[more]

PMID: 27091070

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