Recent advances in the research of HIV-1 RNase H inhibitors.
Reverse transcription is a crucial step in the life cycle of human immunodeficiency virus type 1 (HIV-1). In this process, multiple functional enzymes including RNA-dependent DNA polymerase, DNA-dependent DNA polymerase and RNase H are indispensable. The RNase H functions to degrade RNA of the RNA-DNA heteroduplex into small fragment. These properties of HIV-1 RNase H make it an attractive target for rational anti-HIV-1 drug design and development. In this review, we summarized the HIV-1 RNase H inhibitors that were recently reported in the literature, including their chemical structure, mechanism and structure-activity relationship. It seems likely that HIV-1 RNase H as a prominent non-traditional target may lead to the development of anti-HIV agents which could be used alone or in the combination with other HIV inhibitors in AIDS chemotherapy.
Yu
Fang
F
Institute of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, P.R. China.
Liu
Xinyong
X
Zhan
Peng
P
De Clercq
Erik
E
D000595:Amino Acid Sequence; D019380:Anti-HIV Agents / Q000494:pharmacology*; D020134:Catalytic Domain; D002626:Chemistry, Pharmaceutical / Q000379:methods; D015195:Drug Design; D015658:HIV Infections / Q000188:drug therapy*; D015497:HIV-1 / Q000201:enzymology*; D006801:Humans; D007477:Ions; D008956:Models, Chemical; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016914:Ribonuclease H / Q000378:metabolism*; D013329:Structure-Activity Relationship
D019380:Anti-HIV Agents; D007477:Ions; D016914:Ribonuclease H