Novel aspartyl protease inhibitors, YF-0200R-A and B

T Sato; K Nagai; M Shibazaki; K Abe; Y Takebayashi; B Lumanau; R M Rantiatmodjo

doi:10.7164/antibiotics.47.566

Novel aspartyl protease inhibitors, YF-0200R-A and B

J Antibiot (Tokyo). 1994 May;47(5):566-70. doi: 10.7164/antibiotics.47.566.

Authors

T Sato¹, K Nagai, M Shibazaki, K Abe, Y Takebayashi, B Lumanau, R M Rantiatmodjo

Affiliation

¹ Drug Serendipity Research Laboratories, Yamanouchi Pharmaceutical Co., Ltd., Tokyo, Japan.

PMID: 8040054
DOI: 10.7164/antibiotics.47.566

Abstract

Novel pepstatin A-sensitive Candida albicans aspartyl protease inhibitors, named YF-0200R-A and B, were isolated by column chromatography and preparative HPLC from the fermentation broth of Streptomyces sp. YF-0200R. The structures of YF-0200R-A and B were elucidated by spectroscopic analysis as alpha, beta and gamma, delta unsaturated fatty acids with two or three hydroxyl groups. YF-0200R-A and B inhibit aspartyl protease from Candida albicans with IC50 values of 6.5 x 10(-4) M and 6.2 x 10(-4) M, respectively.

MeSH terms

Aspartic Acid Endopeptidases / antagonists & inhibitors*
Candida albicans / enzymology
Chemical Phenomena
Chemistry, Physical
Fatty Acids, Unsaturated / chemistry*
Fatty Acids, Unsaturated / isolation & purification
Fatty Acids, Unsaturated / pharmacology
Fermentation
Magnetic Resonance Spectroscopy
Molecular Structure
Protease Inhibitors / chemistry*
Protease Inhibitors / isolation & purification
Protease Inhibitors / pharmacology
Streptomyces / chemistry

Substances

Fatty Acids, Unsaturated
Protease Inhibitors
YF 0200R-A
YF 0200R-B
Aspartic Acid Endopeptidases