226998-04-5Relevant articles and documents
Truncation and non-natural amino acid substitution studies on HTLV-I protease hexapeptidic inhibitors
Nguyen, Jeffrey-Tri,Zhang, Meihui,Kumada, Henri-Obadja,Itami, Ayako,Nishiyama, Keiji,Kimura, Tooru,Cheng, Maosheng,Hayashi, Yoshio,Kiso, Yoshiaki
, p. 366 - 370 (2008/09/18)
The culprit behind adult T-cell leukemia, myelopathy/tropical paraparesis, and a plethora of inflammatory diseases is the human T-cell leukemia virus type 1 (HTLV-I). We recently unveiled a potent hexapeptidic HTLV-I protease inhibitor, KNI-10166, compose
Structure-activity and structure-metabolism relationships of HIV protease inhibitors containing the 3-hydroxy-2-methylbenzoyl-allophenylnorstatine structure
Mimoto, Tsutomu,Terashima, Keisuke,Nojima, Satoshi,Takaku, Haruo,Nakayama, Mitsunobu,Shintani, Makoto,Yamaoka, Takashi,Hayashi, Hideya
, p. 281 - 293 (2007/10/03)
A series of peptidomimetic human immunodeficiency virus (HIV) protease inhibitors containing substituted allophenylnorstatine [Apns: (2S,3S)-3-amino-2-hydroxy-4-phenylbutyric acid] were designed and synthesized. From the structure-metabolism relationship of this type of HIV protease inhibitors, the compounds having para substitution of the phenyl ring of Apns and/or 2,6-disubstitution of the P2′ benzylamine were found to be able to avoid the P2 phenol glucuronidation that occurs with SM-319777 (formerly named JE-2147, KNI-764); one of the main metabolic pathways of SM-319777. These new analogues, such as SM-322377, had more desirable pharmacokinetic profiles and more potent antiviral activity against not only wild type HIV-1 but also the multi-drug-resistant HIV-1 than SM-319777.
Tripeptide compounds and anti-AIDS medicine
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, (2008/06/13)
A novel tripeptide compound represented by the following general formula (I) exhibiting superior HIV protease inhibition activity, and an anti-AIDS medicine comprising this compound as an effective component and a pharmaceutically acceptable salt thereof.