Pseudopeptide inhibitors of aminopeptidases containing the Ψ[CH(CN)NH] surrogate as a transition-state MIMIC

  title={Pseudopeptide inhibitors of aminopeptidases containing the $\Psi$[CH(CN)NH] surrogate as a transition-state MIMIC},
  author={M. M. Luisa Sua´rez-Gea and Teresa Garci´a-Lo´pez and Concepcio´n Pe´rez and Rosario Herranz},
  journal={Bioorganic \& Medicinal Chemistry Letters},
2 Citations


Studies on the synthesis of cyanomethyleneamino pseudopeptides
Various cyanomethyleneamino pseudodipeptides were easily prepared in high yield by the Lewis acid catalyzed addition of trimethylsilyl cyanide to unstable aldimine intermediates, obtained from the
Probestin, a new inhibitor of aminopeptidase M, produced by Streptomyces azureus MH663-2F6. I. Taxonomy, production, isolation, physico-chemical properties and biological activities.
Probestin has been isolated as part of a program designed to find microorganism-produced inhibitors of aminopeptidase M from Streptomyces azureus MH663-2F6 and is competitive with the substrate.
Synthesis and structure-activity relationships of bestatin analogues, inhibitors of aminopeptidase B.
In a series of compounds in which the L-leucine residue of bestatin was substituted with other amino acids, only the one containing isoleucine showed more activity than bestatin, and the p-Methyl-, p-chloro-, and p-nitrobestatins showed greater activity.
Synthesis of sulfur-containing analogues of bestatin. Inhibition of aminopeptidases by alpha-thiolbestatin analogues.
The results suggest that the sulfur atoms in 2-thiolbestatin and bestatin thioamide do not interact strongly with the active-site zinc atom of these aminopeptidases when the inhibitors are bound to the enzyme.
Analgesic dipeptide derivatives. 7. 3,7-Diamino-2-hydroxyheptanoic acid (DAHHA) containing dipeptide analogues of the analgesic compound H-Lys-Trp(Nps)-OMe.
The results indicate that the inhibitory capacity of this series of Trp(Nps)-containing dipeptides against enkephalin-degrading enzymes is not an important factor for their antinociceptive effects.
Inhibition of arginine aminopeptidase by bestatin and arphamenine analogues. Evidence for a new mode of binding to aminopeptidases.
Analysis of the synthesis and inhibition kinetics of a new, potent inhibitor of arginine aminopeptidase and structure-activity data for a series of ketomethylene dipeptide isosteres show that the S1 and S1' subsites preferentially bind basic and aromatic side chains, respectively.
Design of novel inhibitors of aminopeptidases. Synthesis of peptide-derived diamino thiols and sulfur replacement analogues of bestatin.
The design rationale and synthesis of novel peptidyl diamino thiol inhibitors of rat brain aminopeptidase are presented, along with accompanying structure-activity analysis, and speculations on the possible mode of enzyme-inhibitor binding of bestatin are offered.
Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes.
papain, chymotrypsin, elastase, acid protease and thermolysin have been found in culture filtrates of actinomycetes. Recently we found that exopeptidases have a strong effect on mammalian cell