S. Kisanuki

Publications15
h-index5
Citations323
Highly Influential Citations2
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Rational design and synthesis of a novel class of active site-targeted HIV protease inhibitors containing a hydroxymethylcarbonyl isostere. Use of phenylnorstatine or allophenylnorstatine as a…
TLDR
A novel class of HIV-1 protease inhibitors containing a hydroxymethylcarbonyl (HMC) isostere were designed from the substrate transition state and synthesized, and incorporation of Pns-Pro or Apns- pro at the P1-P1' site gave potent and specific HIV- 1 prote enzyme inhibitors.
Structure-activity relationship of orally potent tripeptide-based HIV protease inhibitors containing hydroxymethylcarbonyl isostere.
TLDR
A new class of peptidomimetic human immunodeficiency virus protease inhibitors containing a unique unnatural amino acid, allophenylnorstatine, with a hydroxymethylcarbonyl isostere as the active moiety is designed and synthesized.
Kynostatin (KNI)-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.
TLDR
Conformationally constrained tripeptide derivatives, kynostatin (KNI)-227 and -272, exhibited highly potent antiviral activities against a wide spectrum of HIV isolates, indicating that KNI-227 and K NI-272 are promising candidates as selective anti-AIDS drugs.
KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic.
TLDR
Z-Asn-Apns-Pro-NHBut (KNI-102) is the only tripeptide exhibiting substantial anti-HIV activity and may be of minimum size for potent, selective inhibition of HIV protease.
Comparison of a new orally potent tripeptide HIV‐1 protease inhibitor (anti‐aids drug) based on pharmacokinetic characteristics in rats after intravenous and intraduodenal administrations
TLDR
Although the anti‐AIDS virus activity of these two drugs has not been investigated in vivo, KNI‐272 is expected to be a better candidate for oral anti-AIDS therapies.
[Anti-HIV compounds].
Structure-activity relationships of HIV protease inhibitors containing allophenylnorstatine as a transition-state mimic
Structure-activity relationships of HIV protease inhibitors containing hydroxymethylcarbonyl isostere as a transition state mimic
Kynostatin (KNI)‐227 and ‐272, Highly Potent Anti‐HIV Agents: Conformationally Constrained Tripeptide Inhibitors of HIV Protease Containing Allophenylnorstatine.
Design of HIV Protease Inhibitors Based on the Transition State Analogue Concept
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