Journal
MOLECULAR DIVERSITY
Volume 17, Issue 2, Pages 221-243Publisher
SPRINGER
DOI: 10.1007/s11030-013-9424-3
Keywords
VIF-ElonginC interaction inhibition; VEC-5; Anti-HIV-1; Indolizine derivatives; Structure-activity relationship
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Funding
- National Natural Science Foundation of China [20972009]
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The HIV-1 viral infectivity factor (VIF) protein is essential for viral replication. VIF recruits cellular ElonginB/C-Cullin5 E3 ubiquitin ligase to target the host antiviral protein APOBEC3G (A3G) for proteasomal degradation. Thus, the A3G-Vif-E3 complex represents an attractive target for the development of novel anti-HIV drugs. In this study, we describe the design and synthesis of indolizine derivatives as VIF inhibitors targeting the VIF-ElonginC interaction. Many of the synthesized compounds exhibited obvious inhibition activities of VIF-mediated A3G degradation, and 5 compounds showed improvement of activity compared to the known VIF inhibitor VEC-5 (1) with IC values about 20 M. The findings described here will be useful for the development of more potent VIF inhibitors.
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