Hasumi K, Ohyama S, Kohyama T, Ohsaki Y, Takayasu R, Endo A
Department of Applied Biological Science, Tokyo Noko University, Japan.
J Antibiot (Tokyo). 1998 Dec;51(12):1059-68. doi: 10.7164/antibiotics.51.1059.
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 leucine or a tryptophan moiety in respective molecules in place of the N-carboxybutyl portion of the staplabin molecule. SMTP-4, -5, and -6 were active at 0.15 to 0.3 mM in enhancing urokinase-catalyzed plasminogen activation and plasminogen binding to fibrin, as well as plasminogen- and urokinase-mediated fibrinolysis. On the other hand, the concentration of staplabin required to exert such effects was 0.4 to 0.6 mM, and SMTP-3 was inactive at concentrations up to 0.45 mM.
通过溶剂萃取以及使用硅胶柱和硅胶ODS柱进行连续色谱分级分离，从微小葡萄穗霉IFO 30018的培养物中分离出四种新型的三异戊烯基苯酚代谢产物，分别命名为SMTP-3、-4、-5和-6。光谱分析结果表明，SMTP-3、-4、-5和-6是链格孢菌素类似物，在各自分子中分别含有丝氨酸、苯丙氨酸、亮氨酸或色氨酸部分，取代了链格孢菌素分子中的N-羧基丁基部分。SMTP-4、-5和-6在0.15至0.3 mM的浓度下具有活性，可增强尿激酶催化的纤溶酶原激活、纤溶酶原与纤维蛋白的结合，以及纤溶酶原和尿激酶介导的纤维蛋白溶解。另一方面，发挥此类作用所需的链格孢菌素浓度为0.4至0.6 mM，而SMTP-3在浓度高达0.45 mM时无活性。
