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 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.
Drug Serendipity Research Laboratories, Yamanouchi Pharmaceutical Co., Ltd., Tokyo, Japan.
T
T
Sato
K
K
Nagai
M
M
Shibazaki
K
K
Abe
Y
Y
Takebayashi
B
B
Lumanau
R M
RM
Rantiatmodjo
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors*; D002176:Candida albicans / Q000201:enzymology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005231:Fatty Acids, Unsaturated / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D005285:Fermentation; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011480:Protease Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D013302:Streptomyces / Q000737:chemistry
D005231:Fatty Acids, Unsaturated; D011480:Protease Inhibitors; C088531:YF 0200R-A; C088532:YF 0200R-B; D016282:Aspartic Acid Endopeptidases