SMTP-1 and -2, novel analogs of staplabin produced by Stachybotrys microspora IFO30018.
نویسندگان
چکیده
Plasminogen is a circulating zymogen of plasmin, a primary fibrinolytic enzyme1}.Plasminogen binding to fibrin and vascular and blood cells increases the local concentration of the zymogenand accelerates the activation of plasminogen by plasminogen activators2). We have previously isolated a novel fungal triprenyl phenol, designed staplabin, which enhances plasminogen binding to fibrin and cultured cells3). In the present paper, we report the isolation of two novel analogs of staplabin from cultures of Stachybotrys microspora IFO30018. The analogs, designated SMTP-1 and -2, were iso-
منابع مشابه
Activation of fibrinolysis by SMTP-7 and -8, novel staplabin analogs with a pseudosymmetric structure.
Two novel staplabin analogs, SMTP-7 and -8, have been isolated from cultures of Stachybotrys microspora IFO 30018. Spectroscopic analyses showed that the SMTP-7 molecule consisted of two identical staplabin core structures and ornithine which bridges the two partial structures. In the SMTP-8 molecule, the bridging unit was lysine. At concentrations of 80 approximately 150 microM, the two compou...
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Four novel triprenyl phenol metabolites, designated SMTP-3, -4, -5, and -6, have been isolated from cultures of Stachybotrys microspora IFO 30018 by solvent extraction and successive chromatographic fractionation using silica gel and silica ODS columns. A combination of spectroscopic analyses showed that SMTP-3, -4, -5, and -6 are staplabin analogs, containing a serine, a phenylalanine, a leuci...
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BACKGROUND Stachybotrys microspora triprenyl phenols (SMTPs) are a novel family of small molecules that enhance both activation and fibrin-binding of plasminogen. While their effects on fibrinolysis have been characterized in vitro, little is known about their activity in vivo with respect to plasminogen activation and blood clot clearance. RESULTS To select a potent SMTP congener for the eva...
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عنوان ژورنال:
- The Journal of antibiotics
دوره 50 2 شماره
صفحات -
تاریخ انتشار 1997