Mechanism of darunavir binding to monomeric HIV-1 protease: a step forward in the rational design of dimerization inhibitors-Reference-Cited by-同舟云学术

Mechanism of darunavir binding to monomeric HIV-1 protease: a step forward in the rational design of dimerization inhibitors

Published:2022 Issue:11 Volume:24 Page:7107-7120
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ahsan Mohd¹,Pindi Chinmai¹,Senapati Sanjib¹^ORCID

Affiliation:

1. Department of Biotechnology and BJM School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India

Abstract

Binding of Darunavir (DRV) to HIV protease (HIVPR) monomer.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CP/D2CP00024E

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3. Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography

4. Electrostatics Plays a Crucial Role in HIV-1 Protease Substrate Binding, Drugs Fail to Take Advantage

5. A. K.Ghosh , D. D.Anderson and H.Mitsuya , Burger's Medicinal Chemistry and Drug Discovery , John Wiley & Sons, Inc ., Hoboken, NJ, USA , 2010 , pp. 1–74

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