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Identification of a Small-Molecule Inhibitor of HIV-1 Assembly that Targets the Phosphatidylinositol (4,5)-bisphosphate Binding Site of the HIV-1 Matrix Protein
Journal article   Open access   Peer reviewed

Identification of a Small-Molecule Inhibitor of HIV-1 Assembly that Targets the Phosphatidylinositol (4,5)-bisphosphate Binding Site of the HIV-1 Matrix Protein

Isaac Zentner, Luz-Jeannette Sierra, Ayesha K Fraser, Lina Maciunas, Marie K Mankowski, Andrei Vinnik, Peter Fedichev, Roger G Ptak, Julio Martín-García and Simon Cocklin
ChemMedChem, v 8(3), pp 426-432
Mar 2013
PMID: 23361947
url
https://doi.org/10.1002/cmdc.201200577View
Published, Version of Record (VoR) Open

Abstract

HIV-1 matrix proteins virtual screening phosphatidylinositol 4,5-bisphosphates antiviral agents
The development of drug resistance remains a critical problem for current HIV-1 antiviral therapies, creating a need for new inhibitors of HIV-1 replication. We previously reported on a novel anti-HIV-1 compound, N 2 -(phenoxyacetyl)- N -[4-(1-piperidinyl-carbonyl)benzyl]glycinamide ( 14 ), that binds to the highly conserved phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P 2 )binding pocket of the HIV-1 matrix (MA) protein. In this study, we re-evaluate the hits from the virtual screen used to identify compound 14 and test them directly in an HIV-1 replication assay using primary human peripheral blood mononuclear cells. This study resulted in the identification of three new compounds with antiviral activity; 2-(4-{[3-(4-fluorophenyl)-1,2,4-oxadiazol-5-yl]methyl})-1-piperazinyl)- N -(4-methylphenyl)-acetamide ( 7 ), 3-(2-ethoxyphenyl)-5-[[4-(4-nitrophenyl)piperazin-1-yl]methyl]-1,2,4-oxadiazole ( 17 ), and N -[4-ethoxy-3-(1-piperidinylsulfonyl)phenyl]-2-(imidazo[2,1- b ][1,3]thiazol-6-yl)acetamide ( 18 ), with compound 7 being the most potent of these hits. Mechanistic studies on 7 demonstrated that it directly interacts with and functions through HIV-1 MA. In accordance with our drug target, compound 7 competes with PI(4,5)P 2 for MA binding and, as a result, diminishes the production of new virus. Mutation of residues within the PI(4,5)P 2 binding site of MA decreased the antiviral effect of compound 7 . Additionally, compound 7 displays a broadly neutralizing anti-HIV activity, with IC 50 values of 7.5–15.6 μm for the group M isolates tested. Taken together, these results point towards a novel chemical probe that can be used to more closely study the biological role of MA and could, through further optimization, lead to a new class of anti-HIV-1 therapeutics. PIP 2 -ing HIV-1 to the post! The discovery and characterization of a new small-molecule inhibitor (shown) of HIV-1 replication that targets the HIV-1 matrix (MA) protein is described. This novel agent exhibits a broad therapeutic spectrum, inhibiting all of the group M isolates tested, and functions via the novel mechanism of disrupting the critical phosphatidylinositol 4,5-bisphosphate (PI[4,5]P 2 )-MA interaction.

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Collaboration types
International collaboration
Web of Science research areas
Chemistry, Medicinal
Pharmacology & Pharmacy
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