Introduction of polar groups on the naphthalene scaffold of molecular tongs inhibiting wild-type and mutated HIV-1 protease dimerization-Reference-Cited by-同舟云学术

Introduction of polar groups on the naphthalene scaffold of molecular tongs inhibiting wild-type and mutated HIV-1 protease dimerization

Published:2014 Issue:6 Volume:5 Page:719-727
ISSN:2040-2503
Container-title:Med. Chem. Commun.
language:en
Short-container-title:Med. Chem. Commun.

Author:

Fanelli R.¹²³⁴⁵,Ressurreição A. S.¹²³⁴⁵,Dufau L.⁶⁷⁸⁹¹⁰,Soulier J.-L.¹²³⁴⁵,Vidu A.¹²³⁴⁵,Tonali N.¹²³⁴⁵,Bernadat G.¹²³⁴⁵,Reboud-Ravaux M.⁶⁷⁸⁹¹⁰,Ongeri S.¹²³⁴⁵

Affiliation:

1. Molécules Fluorées et Chimie Médicinale

2. BioCIS UMR-CNRS 8076

3. LabEx LERMIT

4. Université Paris-Sud

5. Faculté de Pharmacie

6. Sorbonne Universités

7. UPMC Univ Paris 06

8. UMR 8256

9. B2A

10. Biological Adaptation and Ageing, Integrated Cellular Ageing and Inflammation, Molecular & Functional Enzymology

Abstract

A new series of naphthalene-based molecular tongs containing polar groups at the 3-position of the naphthalene scaffold was synthesized and its anti-dimerization activity was evaluated against HIV-1 protease.

Publisher

Royal Society of Chemistry (RSC)

Subject

Pharmaceutical Science,Biochemistry,Drug Discovery,Molecular Medicine,Pharmacology,Organic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2014/MD/C4MD00032C

Reference59 articles.

1. Active human immunodeficiency virus protease is required for viral infectivity.

2. Toxicity of antiretroviral therapy and implications for drug development

3. Antivirals and antiviral strategies

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