Insights into the structural function of the complex of HIV-1 protease with TMC-126: molecular dynamics simulations and free-energy calculations
D Li, JG Han, H Chen, L Li, RN Zhao, G Liu… - Journal of molecular …, 2012 - Springer
The binding properties of the protein–inhibitor complex of human immunodeficiency virus
type 1 (HIV-1) protease with the inhibitor TMC-126 are investigated by combining …
type 1 (HIV-1) protease with the inhibitor TMC-126 are investigated by combining …
Exploring the drug resistance of V32I and M46L mutant HIV-1 protease to inhibitor TMC114: flap dynamics and binding mechanism
Inhibitors of HIV-1 protease (HIV-1-pr) generally only bind to the active site of the protease.
However, for some mutants such as V32I and M46L the TMC114 can bind not only to the …
However, for some mutants such as V32I and M46L the TMC114 can bind not only to the …
Investigation on the mechanism for the binding and drug resistance of wild type and mutations of G86 residue in HIV-1 protease complexed with Darunavir by …
D Li, Y Zhang, RN Zhao, S Fan, JG Han - Journal of molecular modeling, 2014 - Springer
Residue Gly86 is considered as the highly conversed residue in the HIV-1 protease. In our
work, the detailed binding free energies for the wild-type (WT) and mutated proteases …
work, the detailed binding free energies for the wild-type (WT) and mutated proteases …
Insights into drug resistance of mutations D30N and I50V to HIV-1 protease inhibitor TMC-114: free energy calculation and molecular dynamic simulation
J Chen, S Zhang, X Liu, Q Zhang - Journal of molecular modeling, 2010 - Springer
The single mutations D30N and I50V are considered as the key residue mutations of the HIV-
1 protease drug resistance to inhibitors in clinical use. In this work, molecular dynamics (MD) …
1 protease drug resistance to inhibitors in clinical use. In this work, molecular dynamics (MD) …
Interaction of I50V mutant and I50L/A71V double mutant HIV-protease with inhibitor TMC114 (darunavir): molecular dynamics simulation and binding free energy …
In the present work, the binding of inhibitor TMC114 (darunavir) to wild-type (WT), single
(I50V) as well as double (I50L/A71V) mutant HIV-proteases (HIV-pr) was investigated with …
(I50V) as well as double (I50L/A71V) mutant HIV-proteases (HIV-pr) was investigated with …
Study of the Binding Free Energies between HIV-1 Protease and Its Inhibitors
CH YI, QG ZHANG - Acta Chimica Sinica, 2010 - sioc-journal.cn
HIV-1 protease is an important target of AIDS chemotherapy. Molecular dynamics
simulations followed by MM-PBSA analyses were performed to study the binding of …
simulations followed by MM-PBSA analyses were performed to study the binding of …
Protonation state and free energy calculation of HIV-1 protease–inhibitor complex based on electrostatic polarisation effect
M Yang, X Jiang, N Jiang - Molecular Physics, 2014 - Taylor & Francis
The protonation states of catalytic Asp25/25′ residues remarkably affect the binding
mechanism of the HIV-1 protease–inhibitor complex. Here we report a molecular dynamics …
mechanism of the HIV-1 protease–inhibitor complex. Here we report a molecular dynamics …
Efficiency of a second‐generation HIV‐1 protease inhibitor studied by molecular dynamics and absolute binding free energy calculations
M Lepšík, Z Kříž, Z Havlas - Proteins: Structure, Function, and …, 2004 - Wiley Online Library
ABSTRACT A subnanomolar inhibitor of human immunodeficiency virus type 1 (HIV-1)
protease, designated QF34, potently inhibits the wildtype and drug-resistant enzyme. To …
protease, designated QF34, potently inhibits the wildtype and drug-resistant enzyme. To …
Insight into binding mechanisms of inhibitors MKP56, MKP73, MKP86, and MKP97 to HIV-1 protease by using molecular dynamics simulation
S Shi, S Zhang, Q Zhang - Journal of Biomolecular Structure and …, 2018 - Taylor & Francis
HIV-1 protease (PR) has been a significant target for design of potent inhibitors curing
acquired immunodeficiency syndrome. Molecular dynamics simulations coupled with …
acquired immunodeficiency syndrome. Molecular dynamics simulations coupled with …
Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors …
T Hou, R Yu - Journal of medicinal chemistry, 2007 - ACS Publications
The V82F/I84V double mutation is considered as the key residue mutation of the HIV-1
protease drug resistance because it can significantly lower the binding affinity of protease …
protease drug resistance because it can significantly lower the binding affinity of protease …