Literature DB >> 1423795

Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.

T Mimoto1, J Imai, S Kisanuki, H Enomoto, N Hattori, K Akaji, Y Kiso.   

Abstract

Selective and potent HIV protease inhibitors containing allophenylnorstatine [Apns; (2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric acid] as a transition-state mimic were designed and synthesized. Among them, conformationally constrained tripeptide derivatives, kynostatin (KNI)-227 and -272 (Fig. 1), exhibited highly potent antiviral activities against a wide spectrum of HIV isolates. Ready availability due to the simple synthetic procedure and the excellent antiviral properties indicate that KNI-227 and KNI-272 are promising candidates as selective anti-AIDS drugs.

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Year:  1992        PMID: 1423795     DOI: 10.1248/cpb.40.2251

Source DB:  PubMed          Journal:  Chem Pharm Bull (Tokyo)        ISSN: 0009-2363            Impact factor:   1.645


  8 in total

1.  Metabolic characterization of a tripeptide human immunodeficiency virus type 1 protease inhibitor, KNI-272, in rat liver microsomes.

Authors:  A Kiriyama; T Nishiura; H Yamaji; K Takada
Journal:  Antimicrob Agents Chemother       Date:  1999-03       Impact factor: 5.191

Review 2.  Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS.

Authors:  Arun K Ghosh; Heather L Osswald; Gary Prato
Journal:  J Med Chem       Date:  2016-01-22       Impact factor: 7.446

3.  Ions and inhibitors in the binding site of HIV protease: comparison of Monte Carlo simulations and the linearized Poisson-Boltzmann theory.

Authors:  Dezso Boda; Mónika Valiskó; Douglas Henderson; Dirk Gillespie; Bob Eisenberg; Michael K Gilson
Journal:  Biophys J       Date:  2009-02-18       Impact factor: 4.033

4.  Removal of human immunodeficiency virus type 1 (HIV-1) protease inhibitors from preparations of immature HIV-1 virions does not result in an increase in infectivity or the appearance of mature morphology.

Authors:  R W Humphrey; A Ohagen; D A Davis; T Fukazawa; H Hayashi; S Höglund; H Mitsuya; R Yarchoan
Journal:  Antimicrob Agents Chemother       Date:  1997-05       Impact factor: 5.191

5.  In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine.

Authors:  S Kageyama; T Mimoto; Y Murakawa; M Nomizu; H Ford; T Shirasaka; S Gulnik; J Erickson; K Takada; H Hayashi
Journal:  Antimicrob Agents Chemother       Date:  1993-04       Impact factor: 5.191

6.  Preparation and preliminary characterization of poly(ethylene glycol)-pepstatin conjugate.

Authors:  J Brygier; J Vincentelli; M Nijs; C Guermant; C Paul; D Baeyens-Volant; Y Looze
Journal:  Appl Biochem Biotechnol       Date:  1994-04       Impact factor: 2.926

7.  Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography.

Authors:  Motoyasu Adachi; Takashi Ohhara; Kazuo Kurihara; Taro Tamada; Eijiro Honjo; Nobuo Okazaki; Shigeki Arai; Yoshinari Shoyama; Kaname Kimura; Hiroyoshi Matsumura; Shigeru Sugiyama; Hiroaki Adachi; Kazufumi Takano; Yusuke Mori; Koushi Hidaka; Tooru Kimura; Yoshio Hayashi; Yoshiaki Kiso; Ryota Kuroki
Journal:  Proc Natl Acad Sci U S A       Date:  2009-03-09       Impact factor: 11.205

8.  Protein binding of human immunodeficiency virus protease inhibitor KNI-272 and alteration of its in vitro antiretroviral activity in the presence of high concentrations of proteins.

Authors:  S Kageyama; B D Anderson; B L Hoesterey; H Hayashi; Y Kiso; K P Flora; H Mitsuya
Journal:  Antimicrob Agents Chemother       Date:  1994-05       Impact factor: 5.191

  8 in total

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