HIV-1 gp120 Antagonists Also Inhibit HIV-1 Reverse Transcriptase by Bridging the NNRTI and NRTI Sites.


Journal

Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531

Informations de publication

Date de publication:
25 11 2021
Historique:
pubmed: 5 11 2021
medline: 29 1 2022
entrez: 4 11 2021
Statut: ppublish

Résumé

HIV-1 infection is typically treated using ≥2 drugs, including at least one HIV-1 reverse transcriptase (RT) inhibitor. Drugs targeting RT comprise nucleos(t)ide RT inhibitors (NRTIs) and non-nucleoside RT inhibitors (NNRTIs). NRTI-triphosphates bind at the polymerase active site and, following incorporation, inhibit DNA elongation. NNRTIs bind at an allosteric pocket ∼10 Å away from the polymerase active site. This study focuses on compounds ("NBD derivatives") originally developed to bind to HIV-1 gp120, some of which inhibit RT. We have determined crystal structures of three NBD compounds in complex with HIV-1 RT, correlating with RT enzyme inhibition and antiviral activity, to develop structure-activity relationships. Intriguingly, these compounds bridge the dNTP and NNRTI-binding sites and inhibit the polymerase activity of RT in the enzymatic assays (IC

Identifiants

pubmed: 34735153
doi: 10.1021/acs.jmedchem.1c01104
pmc: PMC10655131
mid: NIHMS1941657
doi:

Substances chimiques

Anti-HIV Agents 0
HIV Envelope Protein gp120 0
Reverse Transcriptase Inhibitors 0
reverse transcriptase, Human immunodeficiency virus 1 EC 2.7.7.-
HIV Reverse Transcriptase EC 2.7.7.49

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

16530-16540

Subventions

Organisme : NIAID NIH HHS
ID : R01 AI027690
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI104416
Pays : United States
Organisme : NIAID NIH HHS
ID : R56 AI104416
Pays : United States

Commentaires et corrections

Type : ErratumIn

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Auteurs

Natalie Losada (N)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.
Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, United States.

Francesc X Ruiz (FX)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.
Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, United States.

Francesca Curreli (F)

Laboratory of Molecular Modeling & Drug Design, Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York 10065, United States.

Kevin Gruber (K)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.
Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, United States.

Alyssa Pilch (A)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.

Kalyan Das (K)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.

Asim K Debnath (AK)

Laboratory of Molecular Modeling & Drug Design, Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York 10065, United States.

Eddy Arnold (E)

Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08854, United States.
Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854, United States.

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Classifications MeSH