OF4949, new inhibitors of aminopeptidase B. I Taxonomy, fermentation, isolation and characterization.

Sano, Susumu; Ikai, Katsushige; Kuroda, Hiroyuki; Nakamura, Teruya; Ôbayashi, Akira; Ezure, Yohji; Enomoto, Hiroshi

doi:10.7164/antibiotics.39.1674

Cited by 50 publications

(12 citation statements)

References 8 publications

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“…In fact, other natural products containing the biaryl-ether junction such as the tripeptide derivatives K13 [45] [46] or OF 4949-I-IV [47] [48] are known inhibitors of metalloproteases. These differ in their structure from the biaryl-ether compounds of this study merely by the presence of a C-terminal carboxy group as the potential ligand of the enzyme metal ion.…”

mentioning

confidence: 99%

TMC‐95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors

Kaiser

Milbradt

Siciliano

et al. 2004

Chemistry & Biodiversity

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TMC-95A, a cyclic tripeptide metabolite of Apiospora montagnei, is a potent competitive inhibitor of proteasome. Based on the X-ray structure of its complex with yeast proteasome, the synthetically challenging structure of this natural product was simplified in a first generation of analogues by replacing the highly oxidized side-chain biaryl system with a phenyl-oxindole group. In the present study, the TMC-95 biaryl group was substituted with a biphenyl ether with retainment of significant proteasome inhibition. Because of the facile synthetic access of tripeptides containing in i, i+2 positions residues of the isodityrosine type, this new generation of TMC-95 analogues may represent promising lead structures for further optimization of affinity and selectivity of proteasome inhibitors.

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confidence: 99%

TMC‐95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors

Kaiser

Milbradt

Siciliano

et al. 2004

Chemistry & Biodiversity

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“…The inhibition by 1 and 2 was not reversed when zinc ion was added. The results indicated that 1 and 2 may act by a mechanism different from the chelating reaction of 1 , Enkephalins are degraded by aminopeptidases18~20) as well as by EKL-A and -B and angiotensinconverting enzyme.21~23) Compound1 strongly inhibited EDAPand EKL-B. From this result, we think that 1 might enhance morphine analgesia, as do bestatin and^-hydroxy-2*S,3i£-3-amino-2-hydroxyphenyl-4-phenylbutanoyl-L-leucine.24)…”

Section: Resultsmentioning

confidence: 88%

OF4949, new inhibitors of aminopeptidase A. IV Effects of OF4949 and its derivatives on enzyme systems.

et al. 1987

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“…Halogenated tyrosine derivatives are constituents of various antibiotics such as piperazinomycins, which shows inhibitory activity against fungi and yeast [33], of K-13 inhibitor of angiotensin-I converting enzyme (ACE) [34], inhibitors of aminopeptidase B [35,36], cephalosporin analogs [37], or naturally occurring peptides [38].…”

Section: N-(2-hydroxyoctyl)- and N-(2-hydroxypropyl)-l-4-hydroxyprmentioning

confidence: 99%

Chiral separation of halogenated amino acids by ligand-exchange capillary electrophoresis

et al. 2005

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The chiral separation of halogenated amino acids by ligand-exchange CE is described. Halogenated amino acids attracted increasing interest in recent years because of their physiological activities. Different chiral selectors, as there are L-4-hydroxyproline, L-histidine, and N-alkyl derivatives of L-4-hydroxyproline in form of their copper(II) complexes, are compared for their chiral recognition ability for halogenated amino acids. The influence of various parameters, such as selector concentration, pH, organic modifier, and field strength, on the resolution was investigated. All halogenated amino acids investigated were baseline-separated under optimized conditions.

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OF4949, new inhibitors of aminopeptidase B. I Taxonomy, fermentation, isolation and characterization.

Cited by 50 publications

References 8 publications

TMC‐95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors

TMC‐95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors

OF4949, new inhibitors of aminopeptidase A. IV Effects of OF4949 and its derivatives on enzyme systems.

Chiral separation of halogenated amino acids by ligand-exchange capillary electrophoresis

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