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JE-2147: a dipeptide protease inhibitor (PI) that potently inhibits multi-PI-resistant HIV-1.
Structural analysis revealed that the presence of a flexible P2' moiety is important for the potency of JE-2147 toward wild-type and mutant viruses, and suggest that the use of flexible components may open a new avenue for designing PIs that resist the emergence of PI-resistant HIV-1.
In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine
Two compounds, K NI-227 and KNI-272, which were highly potent against HIV protease with little inhibition of other aspartic proteases, showed the most potent activity against the infectivity and cytopathic effect of a wide spectrum of HIV strains.
Structure-activity relationship of small-sized HIV protease inhibitors containing allophenylnorstatine.
It is demonstrated that JE-2147 has potent antiviral activities in vitro and exhibits good oral bioavailability and plasma pharmacokinetic profiles in two species of laboratory animals.
A practical use of ligand efficiency indices out of the fragment-based approach: ligand efficiency-guided lead identification of soluble epoxide hydrolase inhibitors.
A practical methodology for lead generation using the concept of ligand efficiency is proposed, which could reveal compounds possessing preferable lead-like characteristics in terms of molecular size and lipophilicity.
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
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.
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.
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.
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.
A new class of amino protecting group removable by reductive acidolysis: the 4-methylsulphinylbenzyloxycarbonyl (Msz) group
A safety-catch type of amino protecting group, the 4-methylsulphinylbenzyloxycarbonyl (Msz) group is stable under both acidic and basic conditions, but can be smoothly removed by a one-pot reaction
KNI‐577, a Potent Small‐Sized HIV Protease Inhibitor Based on the Dipeptide Containing the Hydroxymethylcarbonyl Isostere as an Ideal Transition‐State Mimic
A novel class of HIV protease inhibitors containing allophenylnorstatine with a hydroxymethylcarbonyl (HMC) isostere is designed and synthesized, which exhibited potent in vitro and in vivo antiviral activities with low cytotoxicity.