Interaction of I50V mutant and I50L/A71V double mutant HIV-protease with inhibitor TMC114 (darunavir): molecular dynamics simulation and binding free energy studies.
PMID: 22239286
2012
The journal of physical chemistry. B
Introduction: The resistance of the inhibitor GRL-98065, an analog of TMC114 just aniline group replaced by a 1,3-benzodioxole group, to mutants I50V and V82A was attributed to a higher entropic contribution than in the wild type (WT) HIV-pr, and the reduced van der Waals may be responsible to the drug resistance of I84V to GRL-98065.
Frequency and patterns of protease gene resistance mutations in HIV-infected patients treated with lopinavir/ritonavir as their first protease inhibitor.
PMID: 22258921
2012
The Journal of antimicrobial chemotherapy
Abstract: One or more protease mutations were detected in 32 (11%) patients; the most frequent were I54V (n = 12), M46I (n = 11), V82A (n = 7) and L76V (n = 3).
Potent antiviral HIV-1 protease inhibitor GRL-02031 adapts to the structures of drug resistant mutants with its P1'-pyrrolidinone ring.
PMID: 22401672
2012
Journal of medicinal chemistry
Abstract: Crystal structures at resolutions of 1.25-1.55 A were analyzed for complexes of 1 with the PR containing major drug resistant mutations, PR(I47V), PR(L76V), PR(V82A), and PR(N88D).
Abstract: Mutations of I47V and V82A alter residues in the inhibitor-binding site, while L76V and N88D are distal mutations having no direct contact with the inhibitor.
Abstract: Substitution of a smaller amino acid in PR(I47V) and PR(
HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.
Result: Similarly, mutations in the active site cavity of PR20 (D30N, V32I, I47V and I84V) alter the charge and increase the distance between the flaps and the base of the cavity relative to the values in MDR769 (V82A and I84V).
Low prevalence of transmitted drug resistance in patients newly diagnosed with HIV-1 infection in Sweden 2003-2010.
Result: It must be noted, that three of the patients with developed drug resistance were heavily experienced with reverse transcriptase (RT) and protease (PR) mutations (patient 1: RT: M41L, K103N, M184V, T215S; PR: L10I; patient 2: PR: M41L, V118I, K103N, M184V, L210W, T215S, RT: L10I,
HIV-1 Protease and Substrate Coevolution Validates the Substrate Envelope As the Substrate Recognition Pattern.
PMID: 24348205
2012
Journal of chemical theory and computation
Abstract: In this study, three coevolved protease-substrate complexes (AP2VNC-p1V82A, LP1'Fp1-p6D30N/N88D, and SP3'Np1-p6D30N/N88D) were investigated for structural and dynamic properties by molecular modeling and dynamics simulations.
Conclusion: In this study, structural properties of two drug resistant PR variants (V82A and D30N/N88D) and the substrates that coevolved with these two variants (AP2VNC-p1 and LP1'Fp1-p6/SP3'Np1-p6, respectively) were investigated in conformational ensembles obtained from
Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.
PMID: 23144597
2012
Journal of chemical theory and computation
Abstract: Flap+ is a multi-drug-resistant variant of HIV-1 protease with a combination of mutations at the edge of the active site, within the active site, and in the flaps (L10I, G48V, I54V, V82A).
Introduction: Flap+ is a multi-drug-resistant HIV-1 protease variant with a combination of flap and active site mutations (L10I, G48V, I54V, and V82A) that occur simultaneously in sequences of patients undergoing drug therapy (Figure 1).
Method: As described above, Flap+ contains additional mutations of L10I, G48V, I54V, and
Binding of single walled carbon nanotube to WT and mutant HIV-1 proteases: analysis of flap dynamics and binding mechanism.
PMID: 23142620
2012
Journal of molecular graphics & modelling
Abstract: In the current study we have tested the single-walled carbon nanotube (SWCNT) as an inhibitor in wild type (WT) as well as in three primary mutants (I50V(PR), V82A(PR) and I84V(PR)) of the HIV-1-PR through docking the SWCNT in the active site region, and then performed all-atom MD simulations for the complexes.
Conclusion: The primary objective of this study is to understand the interaction mechanisms of SWCNT and wild type (WT) HIV-1-PR as well as a few primary mutants (I50VPR, V82APR and I84VPR).
Introduction: In the present study, we have tested the SWCNTs as inhibitors in WT as well as in t
Prevalence of HIV drug resistance mutation in the northern Indian population after failure of the first line antiretroviral therapy.
HIV mutation literature information.
PMID: 
2012
The journal of physical chemistry. B
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