Tidwell R R, Geratz J D, Dann O, Volz G, Zeh D, Loewe H
J Med Chem. 1978 Jul;21(7):613-23. doi: 10.1021/jm00205a005.
A series of 62 diarylamidine derivatives was evaluated for their antiproteolytic activity. In all but two of the compounds one or both of the amidino-substituted aryl moieties was either an indole or an indole-like ring. The latter included indene, benzimidazole, benzofuran, benzol[beta]thiophene, and several other related nitrogen-containing heterocycles. Several of the compounds exhibited considerable inhibitory potency against thrombin, trypsin, and pancreatic kallikrein. An outstanding inhibitor of trypsin was found in bis(5-amidino-2-benzimidazolyl)methane (compound 42) with a Ki value of 1.7 X 10(-8) M(pH. 8.1, 37 degrees C). Another derivative, 1,2-di(4-amidino-2-benzofuranyl)ethane (compound 21), proved to be a highly effective inhibitor of the overall blood clotting process. From a general structure-activity standpoint these compounds demonstrate that minor structural variations of low-molecular-weight inhibitors can result in significant changes in specificity and potency with regard to antiproteolytic activity.
对一系列62种二芳基脒衍生物的抗蛋白水解活性进行了评估。除两种化合物外,其余所有化合物的一个或两个脒基取代芳基部分均为吲哚或类吲哚环。后者包括茚、苯并咪唑、苯并呋喃、苯并噻吩以及其他几种相关的含氮杂环。其中几种化合物对凝血酶、胰蛋白酶和胰激肽释放酶表现出相当强的抑制效力。双(5-脒基-2-苯并咪唑基)甲烷(化合物42)是一种出色的胰蛋白酶抑制剂,其Ki值为1.7×10⁻⁸ M(pH 8.1,37℃)。另一种衍生物1,2-二(4-脒基-2-苯并呋喃基)乙烷(化合物21)被证明是整体血液凝固过程的高效抑制剂。从一般的构效关系角度来看,这些化合物表明低分子量抑制剂的微小结构变化可导致抗蛋白水解活性在特异性和效力方面发生显著变化。