Structure-activity relationship of orally potent tripeptide-based HIV protease inhibitors containing hydroxymethylcarbonyl isostere.

…, S Kisanuki, T Fukazawa, K Terashima, R Kato…

Index: Mimoto, Tsutomu; Hattori, Naoko; Takaku, Haruo; Kisanuki, Sumitsugu; Fukazawa, Tominaga; Terashima, Keisuke; Kato, Ryohei; Nojima, Satoshi; Misawa, Satoru; Ueno, Takamasa; Imai, Junya; Enomoto, Hiroshi; Tanaka, Shigeki; Sakikawa, Hiroshi; Shintani, Makoto; Hayashi, Hideya; Kiso, Yoshiaki Chemical and Pharmaceutical Bulletin, 2000 , vol. 48, # 9 p. 1310 - 1326

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Citation Number: 44

Abstract

We designed and synthesized a new class of peptidomimetic human immunodeficiency virus protease inhibitors containing a unique unnatural amino acid, allophenylnorstatine [Apns;(2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric acid], with a hydroxymethylcarbonyl isostere as the active moiety. From a structure-activity relationship study of HIV-1 protease inhibition, enzyme selectivity for other aspartyl proteases, the antiviral activity and ...