Beckmann Anna-Madeleine, Gilberg Erik, Gattner Susanne, Huang Tien L, Vanden Eynde Jean Jacques, Mayence Annie, Bajorath Jürgen, Stirnberg Marit, Gütschow Michael
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany; Department of Life Science Informatics, B-IT, LIMES Program Unit Chemical Biology and Medicinal Chemistry, University of Bonn, Dahlmannstr. 2, 53113 Bonn, Germany.
Bioorg Med Chem Lett. 2016 Aug 1;26(15):3741-5. doi: 10.1016/j.bmcl.2016.05.071. Epub 2016 May 26.
The serine protease matriptase-2 has attracted much attention as a potential target for the treatment of iron overload diseases. In this study, a series of 27 symmetric, achiral bisbenzamidines was evaluated for inhibitory activity against human matriptase-2, against the closely related enzyme human matriptase, as well as against human thrombin, bovine factor Xa and human trypsin. The conformationally restricted piperazine derivative 19 and the oxamide-derived bisbenzamidine 1 were identified as the most potent inhibitors of this series for matriptase-2 and matriptase, respectively.
丝氨酸蛋白酶matriptase-2作为治疗铁过载疾病的潜在靶点已备受关注。在本研究中，对一系列27种对称、无手性的双苯甲脒进行了评估，以检测其对人matriptase-2、密切相关的酶人matriptase以及人凝血酶、牛因子Xa和人胰蛋白酶的抑制活性。构象受限的哌嗪衍生物19和草酰胺衍生的双苯甲脒1分别被确定为该系列中对matriptase-2和matriptase最有效的抑制剂。
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