NOVEL ASPARTYL PROTEASE INHIBITORS, YF-0200R-A and B

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 α,...

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Veröffentlicht in:	Journal of antibiotics 1994/05/25, Vol.47(5), pp.566-570
Hauptverfasser:	SATO, TSUTOMU, NAGAI, KOJI, SHIBAZAKI, MITSUYOSHI, ABE, KENJI, TAKEBAYASHI, YUKIHIRO, LUMANAU, BUD, RANTIATMODJO, RATNA MURNI
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartic Acid Endopeptidases - antagonists & inhibitors Biological and medical sciences Candida albicans - enzymology Chemical Phenomena Chemistry, Physical Fatty Acids, Unsaturated - chemistry Fatty Acids, Unsaturated - isolation & purification Fatty Acids, Unsaturated - pharmacology Fermentation General pharmacology Magnetic Resonance Spectroscopy Medical sciences Molecular Structure Pharmacognosy. Homeopathy. Health food Pharmacology. Drug treatments Protease Inhibitors - chemistry Protease Inhibitors - isolation & purification Protease Inhibitors - pharmacology Streptomyces Streptomyces - chemistry
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Zusammenfassung:	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 α, β and γ, δ unsaturated fatty acids with two or three hydroxyl groups. YF-0200R-A and B inhibit aspartyl protease from Candida albicans with IC50 values of 6.5×10-4M and 6.2×10-4M, respectively.
ISSN:	0021-8820 1881-1469
DOI:	10.7164/antibiotics.47.566