TMC-52A to D, novel cysteine proteinase inhibitors, produced by Gliocladium sp

J Antibiot (Tokyo). 1998 Jul;51(7):629-34. doi: 10.7164/antibiotics.51.629.

Abstract

New cysteine proteinase inhibitors, TMC-52A, B, C, and D, were isolated from the fungal fermentation broth. On the basis of a taxonomical study, the producing strain, F-2665, was characterized as Gliocladium sp. Spectroscopic analyses and chemical degradation have shown TMC-52A to D to be epoxysuccinyl peptides. TMC-52A to D strongly inhibited cysteine proteinases, in particular, cathepsin L with IC50 values of 13 nM, 10nM, 10nM, and 6nM, respectively.

MeSH terms

  • Cathepsin L
  • Cathepsins / antagonists & inhibitors*
  • Cysteine Endopeptidases
  • Cysteine Proteinase Inhibitors* / biosynthesis
  • Cysteine Proteinase Inhibitors* / chemistry
  • Cysteine Proteinase Inhibitors* / isolation & purification
  • Cysteine Proteinase Inhibitors* / pharmacology
  • Endopeptidases*
  • Magnetic Resonance Spectroscopy
  • Mass Spectrometry
  • Mitosporic Fungi / chemistry*
  • Mitosporic Fungi / classification
  • Mitosporic Fungi / metabolism
  • Molecular Structure
  • Phenylalanine / analogs & derivatives*
  • Phenylalanine / chemical synthesis
  • Phenylalanine / chemistry
  • Phenylalanine / isolation & purification
  • Phenylalanine / pharmacology
  • Succinates* / chemical synthesis
  • Succinates* / chemistry
  • Succinates* / isolation & purification*
  • Succinates* / pharmacology
  • Tyrosine / analogs & derivatives*
  • Tyrosine / chemical synthesis
  • Tyrosine / chemistry
  • Tyrosine / isolation & purification*
  • Tyrosine / pharmacology

Substances

  • Cysteine Proteinase Inhibitors
  • Succinates
  • TMC 52A
  • TMC 52B
  • TMC 52C
  • TMC 52D
  • Tyrosine
  • Phenylalanine
  • Cathepsins
  • Endopeptidases
  • Cysteine Endopeptidases
  • Cathepsin L