scholarly journals Kinetic and thermodynamic characterisation of HIV-protease inhibitors against E35D↑G↑S mutant in the South African HIV-1 subtype C protease

2019 ◽  
Vol 34 (1) ◽  
pp. 1451-1456 ◽  
Author(s):  
Sibusiso Maseko ◽  
Eden Padayachee ◽  
Siyabonga Maphumulo ◽  
Thavendran Govender ◽  
Yasien Sayed ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
South African ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Subtype C ◽  
The South ◽  
Hiv 1

Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistance

2013 ◽  
Vol 31 (12) ◽  
pp. 1370-1380 ◽  
Author(s):  
Previn Naicker ◽  
Ikechukwu Achilonu ◽  
Sylvia Fanucchi ◽  
Manuel Fernandes ◽  
Mahmoud A.A. Ibrahim ◽  
...  
Keyword(s):  
Drug Resistance ◽  
South African ◽  
Hinge Region ◽  
Subtype C ◽  
The South ◽  
Structural Insights ◽  
Hiv 1

HIV protease inhibitors with picomolar potency against PI-Resistant HIV-1 by extension of the P3 substituent

2003 ◽  
Vol 13 (15) ◽  
pp. 2569-2572 ◽  
Author(s):  
Joseph L. Duffy ◽  
Thomas A. Rano ◽  
Nancy J. Kevin ◽  
Kevin T. Chapman ◽  
William A. Schleif ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Hiv 1

EMERGENCE OF DRUG RESISTANCE IN HIV-1 SUBTYPE C INFECTED CHILDREN FAILING THE SOUTH AFRICAN NATIONAL ANTIRETROVIRAL ROLL-OUT PROGRAM

2009 ◽  
Vol 28 (12) ◽  
pp. 1123-1125 ◽  
Author(s):  
Carole L. Wallis ◽  
Linda Erasmus ◽  
Sheba Varughese ◽  
Dalu Ndiweni ◽  
Wendy S. Stevens
Keyword(s):  
Drug Resistance ◽  
South African ◽  
Subtype C ◽  
The South ◽  
Hiv 1 ◽  
Roll Out

Reduction of Peptide Character of HIV Protease Inhibitors That Exhibit Nanomolar Potency against Multidrug Resistant HIV-1 Strains

2003 ◽  
Vol 46 (9) ◽  
pp. 1764-1768 ◽  
Author(s):  
Hirokazu Tamamura ◽  
Yasuhiro Koh ◽  
Satoshi Ueda ◽  
Yoshikazu Sasaki ◽  
Tomonori Yamasaki ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Multidrug Resistant ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Hiv 1

scholarly journals Antiviral activity of the dihydropyrone PNU-140690, a new nonpeptidic human immunodeficiency virus protease inhibitor.

1997 ◽  
Vol 41 (5) ◽  
pp. 1058-1063 ◽  
Author(s):  
S M Poppe ◽  
D E Slade ◽  
K T Chong ◽  
R R Hinshaw ◽  
P J Pagano ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Antiviral Activity ◽  
Protease Inhibitors ◽  
Hiv Protease ◽  
Pharmacokinetic Studies ◽  
Hiv Protease Inhibitors ◽  
Highly Active ◽  
Immunodeficiency Virus ◽  
Hiv 1

PNU-140690 is a member of a new class of nonpeptidic human immunodeficiency virus (HIV) protease inhibitors (sulfonamide-containing 5,6-dihydro-4-hydroxy-2-pyrones) discovered by structure-based design. PNU-140690 has excellent potency against a variety of HIV type 1 (HIV-1) laboratory strains and clinical isolates, including those resistant to the reverse transcriptase inhibitors zidovudine or delavirdine. When combined with either zidovudine or delavirdine, PNU-140690 contributes to synergistic antiviral activity. PNU-140690 is also highly active against HIV-1 variants resistant to peptidomimetic protease inhibitors, underscoring the structural distinctions between PNU-140690 and substrate analog protease inhibitors. PNU-140690 retains good antiviral activity in vitro in the presence of human plasma proteins, and preclinical pharmacokinetic studies revealed good oral bioavailability. Accordingly, PNU-140690 is a candidate for clinical evaluation.

scholarly journals Applications of Click Chemistry in the Development of HIV Protease Inhibitors

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Mukesh M. Mudgal ◽  
Nagaraju Birudukota ◽  
Mayur A. Doke
Keyword(s):  
Protease Inhibitor ◽  
Click Chemistry ◽  
Protease Inhibitors ◽  
Highly Active Antiretroviral Therapy ◽  
Click Reaction ◽  
Large Body ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Infected People ◽  
Hiv 1

Acquired Immunodeficiency Syndrome (AIDS) has been devastating for millions of people around the world. Inhibition of the human immunodeficiency virus (HIV) protease is among the most important approaches for the therapeutic intervention in HIV infection. Since the discovery of the HIV-1 protease, this enzyme has been considered as a key target for the inhibition of viral replication. A large body of research has been done to develop an effective HIV-1 protease inhibitor. There are to date 10 HIV-1 protease inhibitor drugs approved by the Food and Drug Administration (FDA) that have improved the survival and quality of life of HIV infected people. These drugs are prescribed in combination with the reverse transcriptase inhibitors, which is referred to as highly active antiretroviral therapy (HAART). The HIV-1 protease inhibitors play a vital role in HAART. The applications of click chemistry are dispersing in the field of drug discovery. Recently, click chemistry has captured a lot of attention and has become a powerful tool for the synthesis of medicinal skeletons in the discovery of anti-HIV drugs. Click reaction is a well-known method for making carbon−heteroatom−carbon bonds. Click reactions are popular because they are wide in scope, of high yielding, quick to perform, and easy to purify. In this review, we outlined current approaches towards the development of HIV-1 protease inhibitors employing click chemistry.

Determining and Overcoming Resistance to HIV Protease Inhibitors

2004 ◽  
Vol 4 (2) ◽  
pp. 137-152 ◽  
Author(s):  
Jana Prejdova ◽  
Milan Soucek ◽  
Jan Konvalinka
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors
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