TMC-52A to D, novel cysteine proteinase inhibitors, produced by Gliocladium sp.
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.
Isshiki
K
K
Lead Generation Research Laboratory at Toda, Tanabe Seiyaku Co., Ltd., Saitama, Japan.
Nishio
M
M
Sakurai
N
N
Uchida
T
T
Okuda
T
T
Komatsubara
S
S
D056668:Cathepsin L; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D003546:Cysteine Endopeptidases; D015853:Cysteine Proteinase Inhibitors / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D010450:Endopeptidases; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D003904:Mitosporic Fungi / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D015394:Molecular Structure; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D013386:Succinates / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology
D015853:Cysteine Proteinase Inhibitors; D013386:Succinates; C114132:TMC 52A; C114133:TMC 52B; C114134:TMC 52C; C114135:TMC 52D; D014443:Tyrosine; D010649:Phenylalanine; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L