@article{oai:repo.qst.go.jp:00049236,
 author = {Hidaka, Koushi and Kimura, Tooru and Sankaranarayanan, Rajesh and Wang, Jun and F. McDaniel, Keith and J. Kempf, Dale and Kameoka, Masanori and Adachi, Motoyasu and Kuroki, Ryota and Jeffrey-Tri, Nguyen and Hayashi, Yoshio and Kiso, Yoshiaki and Adachi, Motoyasu},
 issue = {12},
 journal = {Journal of Medicinal Chemistry},
 month = {Nov},
 note = {The emergence of drug-resistant HIV from a wide spreading anti-viral chemotherapy targeting the HIV protease in the past decades is unavoidable and provides a challenge to develop alternative inhibitors. We synthesized a series of allophenylnorstatine-based peptidomimetics with various P3, P2 and P2´ moieties. The derivatives with P2 tetrahydrofuranylglycine (Thfg) were found to be potent against wild type HIV-1 protease and the virus, identifying a highly potent compound 21f (KNI-1657) against lopinavir/ritonavir- or darunavir-resistant strains. Co-crystal structures of 21f and the wild-type protease revealed numerous key hydrogen bonding interactions with the Thfg. These results suggest that the strategy to design allophenylnorstatine-based peptidomimetics combined with Thfg residue would be promising for generating candidates to overcome multi-drug resistance.},
 pages = {5138--5153},
 title = {Identification of Highly Potent Human Immunodeficiency Virus Type-1 Protease Inhibitors against Lopinavir and Darunavir Resistant Viruses from Allophenylnorstatine-Based Peptidomimetics with P2 Tetrahydrofuranylglycine},
 volume = {61},
 year = {2018}
}