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kynostatin 272

Known as: 4-Thiazolidinecarboxamide, N-(1,1-dimethylethyl)-3- [2-hydroxy-3-[[2-[[(5-isoquinolinyloxy)acetyl]amino]-3- (methylthio)-1-oxopropyl]amino]-1-oxo-4-phenylbutyl]-,[4R-[3[2S*, 3S*(R*)],4R*]], KNI-272, kynostatin-272 
A synthetic peptide-based antiviral agent. As a peptidomimetic substrate containing an unnatural amino acid, allophenylnorstatine, KNI-272… 
National Institutes of Health

Related topics

Related topics

3 relations

Broader (3)

Anti-HIV AgentsHIV Protease InhibitorsOligopeptides

Papers overview

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Highly Cited
2002
Highly Cited
2002
Amino Acid Substitutions in Gag Protein at Non-cleavage Sites Are Indispensable for the Development of a High Multitude of HIV-1 Resistance against Protease Inhibitors*
Amino acid substitutions in human immunodeficiency virus type 1 (HIV-1) Gag cleavage sites have been identified in HIV-1 isolated… 
Highly Cited
2000
Highly Cited
2000
Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitor
KNI‐272 is a powerful HIV‐1 protease inhibitor with a reported inhibition constant in the picomolar range. In this paper, a… 
Highly Cited
1999
Highly Cited
1999
JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.
We designed, synthesized, and identified JE-2147, an allophenylnorstatine-containing dipeptide HIV protease inhibitor (PI), which… 
Highly Cited
1999
Highly Cited
1999
Thermodynamic linkage between the binding of protons and inhibitors to HIV‐1 protease
The aspartyl dyad of free HIV‐1 protease has apparent pKas of ∼3 and ∼6, but recent NMR studies indicate that the aspartyl dyad… 
Highly Cited
1998
Highly Cited
1998
Relative potency of protease inhibitors in monocytes/macrophages acutely and chronically infected with human immunodeficiency virus.
The activity of three human immunodeficiency virus (HIV) protease inhibitors was investigated in human primary monocytes… 
Highly Cited
1996
Highly Cited
1996
Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272.
In order to improve the design of HIV-1 protease inhibitors, it is essential to understand how they interact with active site… 
Highly Cited
1995
Highly Cited
1995
Kinetic characterization and cross-resistance patterns of HIV-1 protease mutants selected under drug pressure.
Eleven different recombinant, drug-resistant HIV-1 protease (HIV PR) mutants--R8Q, V32I, M46I, V82A, V82F, V82I, I84V, V32I/I84V… 
Highly Cited
1995
Highly Cited
1995
Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatine.
Highly Cited
1993
Highly Cited
1993
In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine
Transition state mimetic tripeptide human immunodeficiency virus (HIV) protease inhibitors containing allophenylnorstatine [(2S… 
Highly Cited
1992
Highly Cited
1992
Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.
Selective and potent HIV protease inhibitors containing allophenylnorstatine [Apns; (2S, 3S)-3-amino-2-hydroxy-4-phenylbutyric… 
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