Dynamics of “Flap” Structures in Three HIV-1 Protease/Inhibitor Complexes Probed by Total Chemical Synthesis and Pulse-EPR Spectroscopy

2009 ◽  
Vol 131 (3) ◽  
pp. 884-885 ◽  
Author(s):  
Vladimir Yu. Torbeev ◽  
H. Raghuraman ◽  
Kalyaneswar Mandal ◽  
Sanjib Senapati ◽  
Eduardo Perozo ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Protease Inhibitor ◽  
Epr Spectroscopy ◽  
Pulse Epr ◽  
Hiv 1

A new class of HIV-1 protease inhibitor: The crystallographic structure, inhibition and chemical synthesis of an aminimide peptide isostere

1996 ◽  
Vol 4 (9) ◽  
pp. 1545-1558 ◽  
Author(s):  
Earl E. Rutenber ◽  
Fiona McPhee ◽  
Alan P. Kaplan ◽  
Steven L. Gallion ◽  
Joseph C. Hogan ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Protease Inhibitor ◽  
Crystallographic Structure ◽  
New Class ◽  
Hiv 1

Molecular Docking, Synthesis and anti-HIV-1 Protease Activity of Novel Chalcones

2020 ◽  
Vol 26 (8) ◽  
pp. 802-814 ◽  
Author(s):  
Nemanja Turkovic ◽  
Branka Ivkovic ◽  
Jelena Kotur-Stevuljevic ◽  
Milica Tasic ◽  
Bojan Marković ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Molecular Docking ◽  
Chemical Synthesis ◽  
Protease Activity ◽  
Molecular Mechanisms ◽  
Replication Cycle ◽  
Low Molecular Weight ◽  
Chalcone Derivatives ◽  
Anti Hiv ◽  
Hiv 1

Background: Since the beginning of the HIV/AIDS epidemic, 75 million people have been infected with the HIV and about 32 million people have died of AIDS. Investigation of the molecular mechanisms critical to the HIV replication cycle led to the identification of potential drug targets for AIDS therapy. One of the most important discoveries is HIV-1 protease, an enzyme that plays an essential role in the replication cycle of HIV. Objective: The aim of the present study is to synthesize and investigate anti-HIV-1 protease activity of some chalcone derivatives with the hope of discovering new lead structure devoid drug resistance. Methods: 20 structurally similar chalcone derivatives were synthesized and their physico-chemical characterization was performed. Binding of chalcones to HIV-1 protease was investigated by fluorimetric assay. Molecular docking studies were conducted to understand the interactions. Results: The obtained results revealed that all compounds showed anti-HIV-1 protease activity. Compound C1 showed the highest inhibitory activity with an IC50 value of 0.001 μM, which is comparable with commercial product Darunavir. Conclusion: It is difficult to provide general principles of inhibitor design. Structural properties of the compounds are not the only consideration; ease of chemical synthesis, low molecular weight, bioavailability, and stability are also of crucial importance. Compared to commercial products the main advantage of compound C1 is the ease of chemical synthesis and low molecular weight. Furthermore, compound C1 has a structure that is different to peptidomimetics, which could contribute to its stability and bioavailability.

EPR Spectroscopy Elucidates the Electronic Structure of [FeV(O)(TAML)] Complexes

2021 ◽  
Author(s):  
Yujeong Kim ◽  
Jin Kim ◽  
Linh. K. Nguyen ◽  
Yong-Min Lee ◽  
Wonwoo Nam ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Epr Spectroscopy ◽  
Macrocyclic Ligands ◽  
Spin Hamiltonian ◽  
Pulse Epr ◽  
Hamiltonian Parameters

Multifrequency, multitechnique pulse EPR spectroscopy was employed to unravel the spin Hamiltonian parameters of 17O in the [FeV=O] moiety with two different tetraamido macrocyclic ligands (TAMLs), [FeV(O)(TAML-1)]– (1, H4(TAML-1) =...

scholarly journals Simplification Therapy with Once‐Daily Emtricitabine, Didanosine, and Efavirenz in HIV‐1–Infected Adults with Viral Suppression Receiving a Protease Inhibitor–Based Regimen: A Randomized Trial

2005 ◽  
Vol 191 (6) ◽  
pp. 830-839 ◽  
Author(s):  
Jean‐Michel Molina ◽  
Valérie Journot ◽  
Laurence Morand‐Joubert ◽  
Patrick Yéni ◽  
Willy Rozenbaum ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Randomized Trial ◽  
Viral Suppression ◽  
Once Daily ◽  
Hiv 1

scholarly journals Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy

2021 ◽  
Author(s):  
Aidin R. Balo ◽  
Lizhi Tao ◽  
R. David Britt
Keyword(s):  
Epr Spectroscopy ◽  
Continuous Wave ◽  
Spectroscopic Studies ◽  
Paramagnetic Species ◽  
Paramagnetic Resonance ◽  
Iron Sulfur Cluster ◽  
Radical Sam Enzymes ◽  
Iron Sulfur ◽  
Pulse Epr ◽  
Multiple Domains

AbstractOwing to their importance, diversity and abundance of generated paramagnetic species, radical S-adenosylmethionine (rSAM) enzymes have become popular targets for electron paramagnetic resonance (EPR) spectroscopic studies. In contrast to prototypic single-domain and thus single-[4Fe–4S]-containing rSAM enzymes, there is a large subfamily of rSAM enzymes with multiple domains and one or two additional iron–sulfur cluster(s) called the SPASM/twitch domain-containing rSAM enzymes. EPR spectroscopy is a powerful tool that allows for the observation of the iron–sulfur clusters as well as potentially trappable paramagnetic reaction intermediates. Here, we review continuous-wave and pulse EPR spectroscopic studies of SPASM/twitch domain-containing rSAM enzymes. Among these enzymes, we will review in greater depth four well-studied enzymes, BtrN, MoaA, PqqE, and SuiB. Towards establishing a functional consensus of the additional architecture in these enzymes, we describe the commonalities between these enzymes as observed by EPR spectroscopy.

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