Anti-Aids Agents, 2: Inhibitory Effect of Tannins on HIV Reverse Transcriptase and HIV Replication in H9 Lymphocyte Cells

1990 ◽  
Vol 53 (3) ◽  
pp. 587-595 ◽  
Author(s):  
Gen-ichiro Nonaka ◽  
Itsuo Nishioka ◽  
Makoto Nishizawa ◽  
Takashi Yamagishi ◽  
Yoshiki Kashiwada ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Inhibitory Effect ◽  
Hiv Reverse Transcriptase ◽  
Hiv Replication

A Homodimeric Sporamin-Type Trypsin Inhibitor with Antiproliferative, HIV Reverse Transcriptase-Inhibitory and Antifungal Activities from Wampee (Clausena lansium) Seeds

2003 ◽  
Vol 384 (2) ◽  
pp. 289-293 ◽  
Author(s):  
T.B. Ng ◽  
S.K. Lam ◽  
W.P. Fong
Keyword(s):  
Reverse Transcriptase ◽  
Trypsin Inhibitor ◽  
Simple Procedure ◽  
Inhibitory Effect ◽  
Exchange Chromatography ◽  
Proteinase K ◽  
Human Leukemia ◽  
Hiv Reverse Transcriptase ◽  
Rabbit Reticulocyte Lysate System ◽  
Reticulocyte Lysate

Abstract A homodimeric trypsin inhibitor with a molecular mass of 54 kDa was isolated from the seeds of Clausena lansium (Lour) Skeels with a very simple procedure comprising extraction with an aqueous buffer and ion exchange chromatography on CM-cellulose. It inhibited trypsin with an IC50 of 2.2 nM but was without any inhibitory effect on chymotrypsin and proteinase K. The uptake of MTT by human leukemia HL60 and hepatoma Hep G2 cells was inhibited with an IC50 of 100 uM. Translation in the cellfree rabbit reticulocyte lysate system was inhibited with an IC50 of 3.6 uM. The activity of HIV-1 reverse transcriptase was reduced in the presence of the trypsin inhibitor. The trypsin inhibitor exerted antifungal activity toward Physalospora piricola but not Mycosphaerella arachidicola, Botrytis cinerea, Fusarium oxysporum or Coprinus comatus.

scholarly journals Structure-Based Design of Novel Dihydroalkoxybenzyloxopyrimidine Derivatives as Potent Nonnucleoside Inhibitors of the Human Immunodeficiency Virus Reverse Transcriptase

1998 ◽  
Vol 42 (12) ◽  
pp. 3225-3233 ◽  
Author(s):  
Elise A. Sudbeck ◽  
Chen Mao ◽  
Rakesh Vig ◽  
T. K. Venkatachalam ◽  
Lisa Tuel-Ahlgren ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Reverse Transcriptase ◽  
Mononuclear Cells ◽  
Binding Pocket ◽  
Hiv Reverse Transcriptase ◽  
Hiv Replication ◽  
Peripheral Blood Mononuclear ◽  
Immunodeficiency Virus ◽  
Anti Hiv ◽  
Potent Inhibitory Activity

ABSTRACT Two highly potent dihydroalkoxybenzyloxopyrimidine (DABO) derivatives targeting the nonnucleoside inhibitor (NNI) binding site of human immunodeficiency virus (HIV) reverse transcriptase (RT) have been designed based on the structure of the NNI binding pocket and tested for anti-HIV activity. Our lead DABO derivative, 5-isopropyl-2-[(methylthiomethyl)thio]-6-(benzyl)-pyrimidin-4-(1H)-one, elicited potent inhibitory activity against purified recombinant HIV RT and abrogated HIV replication in peripheral blood mononuclear cells at nanomolar concentrations (50% inhibitory concentration, <1 nM) but showed no detectable cytotoxicity at concentrations as high as 100 μM.

scholarly journals Reverse Transcriptase-Associated Ribonuclease H Activity as a Target for Antiviral Chemotherapy

1997 ◽  
Vol 8 (3) ◽  
pp. 173-185 ◽  
Author(s):  
JW Rausch ◽  
SFJ Le Grice
Keyword(s):  
Reverse Transcriptase ◽  
Therapeutic Intervention ◽  
Rnase H ◽  
Ribonuclease H ◽  
Hiv Reverse Transcriptase ◽  
Recombinant Enzymes ◽  
Hiv Replication ◽  
Precise Evaluation ◽  
Immunodeficiency Virus ◽  
Antiviral Chemotherapy

The availability of highly purified recombinant enzymes and model heteropolymeric nucleic acid substrates now allows more precise evaluation of the ribonuclease H (RNase H) activity associated with human immunodeficiency virus (HIV) reverse transcriptase. In addition to degrading the RNA–DNA replicative intermediate, this C-terminal domain of around 130 residues supports highly specialized events that cannot be complemented by host-coded enzymes during retrovirus replication. RNase H activity should therefore be considered a plausible candidate for therapeutic intervention. Events during HIV replication requiring precise RNase H-mediated hydrolysis, the methodologies available to study these events, and their potential for therapeutic intervention are reviewed here.

RNA aptamers and HIV reverse transcriptase : molecular basis of their interactions and the evaluation of aptamer resistance

2019 ◽  
Author(s):  
◽  
Phuong Dinh Minh Nguyen
Keyword(s):  
Reverse Transcriptase ◽  
Reverse Transcription ◽  
Immune Deficiency Syndrome ◽  
Inhibitory Effect ◽  
Proteolytic Processing ◽  
Rna Aptamers ◽  
Rna Aptamer ◽  
Hiv Reverse Transcriptase ◽  
Functional Features ◽  
Hiv Rt

[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] Human Immunodeficiency virus (HIV) is a pandemic Lentivirus that causes acquired immune deficiency syndrome (AIDS) in infected individuals. One of the critical steps in HIV replication is the reverse transcription of viral RNA to generate viral DNA, which will be integrated into the host genome to generate materials for the production of new viruses. The enzyme responsible for this reverse transcription process is HIV reverse transcriptase (RT). Because of its importance in HIV life cycle, RT has been a common target for HIV inhibitors. In recent years, RNA aptamers have emerged as potential inhibitors against HIV RT. Although previous studies had shown that the inhibitory effect of RNA aptamers against HIV RT comes from their ability to compete with primer/template for binding to RT, the molecular details of RT-RNA aptamer interaction are still limited. The work described herein highlights advancements in identifying the functional features of a broad-spectrum RNA aptamer and elucidating the molecular details in the interaction of this aptamer and the target RT. Furthermore, this work explores the potential use of anti HIV aptamers in studying RT maturation by proteolytic processing.

Inhibitory effect against polymerase and ribonuclease activities of HIV-reverse transcriptase of the aqueous leaf extract ofTerminalia triflora

2002 ◽  
Vol 16 (8) ◽  
pp. 778-780 ◽  
Author(s):  
V. S. Martino ◽  
P. López ◽  
J. J. Martinez Irujo ◽  
M. Sanromán ◽  
M. T. Cuevas ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Leaf Extract ◽  
Inhibitory Effect ◽  
Hiv Reverse Transcriptase ◽  
Aqueous Leaf Extract

scholarly journals Inhibitory Effect of 2,3,5,6-Tetrafluoro-4-[4-(aryl)-1H-1,2,3-triazol-1-yl]benzenesulfonamide Derivatives on HIV Reverse Transcriptase Associated RNase H Activities

2016 ◽  
Vol 17 (8) ◽  
pp. 1371 ◽  
Author(s):  
Nicolino Pala ◽  
Francesca Esposito ◽  
Dominga Rogolino ◽  
Mauro Carcelli ◽  
Vanna Sanna ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Inhibitory Effect ◽  
Rnase H ◽  
Hiv Reverse Transcriptase

New Efavirenz Derivatives and 1,2,3-Triazolyl-phosphonates as Inhibitors of Reverse Transcriptase of HIV-1

2018 ◽  
Vol 18 (17) ◽  
pp. 1494-1505 ◽  
Author(s):  
Carolina C.P. Costa ◽  
Nubia Boechat ◽  
Monica M. Bastos ◽  
Fernando de C. da Silva ◽  
Andressa Marttorelli ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Triazole Ring ◽  
Biological Evaluation ◽  
World Health ◽  
Hiv Reverse Transcriptase ◽  
Ic50 Values ◽  
Health Organization ◽  
Hiv Drugs ◽  
Immunodeficiency Syndrome ◽  
New Compounds

Background: According to the World Health Organization (WHO), the fight against Acquired Immunodeficiency Syndrome (AIDS) is still one of the most significant challenges facing humanity. Worldwide, it is estimated that 36.7 million people are infected by the Human Immunodeficiency Virus (HIV). Despite the variety of available drugs, the search for new enzymatic inhibitors of HIV is still important due to the presence of adverse effects and the development of resistant strains. Therefore, the present study aimed to design, synthesize, and biologically evaluate novel inhibitors of HIV Reverse Transcriptase (RT). Materials and Methods: These compounds were obtained in two series, and compounds in both series contain a 1,2,3-triazole ring in their structures. The compounds in the first series are Efavirenz (EFV) analogues with the N-1 position substituted by another important fragment as described in the medicinal chemistry literature on anti-HIV drugs. The second series has a phosphonate chain similar to that in the structure of Tenofovir Disoproxil Fumarate (TDF). Results and Conclusion: The results of the biological evaluation showed that all compounds presented high RT inhibition values and lower or comparable inhibitory concentrations (the concentration needed to reduce the enzymatic activity by 50%, IC50 values, 0.8-1.9 µM). Among the compounds in the first series, the three with the lowest IC50 values had values between 0.8-0.9 µM, and of those in the second series, the most potent had an IC50 value of 1.1 µM; compounds in both series were equipotent to TDF (1.2 µM). Thus, the new compounds could be considered lead compounds for the development of new antiretroviral compounds.

scholarly journals Interaction of HIV reverse transcriptase with structures mimicking recombination intermediates.

2003 ◽  
Vol 278 (30) ◽  
pp. 28354-28355
Author(s):  
Aarti Raja ◽  
Jeffrey J. DeStefano
Keyword(s):  
Reverse Transcriptase ◽  
Hiv Reverse Transcriptase
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