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.
Institute of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, Jinan, P.R. China.
Fang
F
Yu
Xinyong
X
Liu
Peng
P
Zhan
Erik
E
De Clercq
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