Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Tykistökatu 6A, FI-20520 Turku, Finland.
MediCity Research Laboratory, University of Turku, Tykistökatu 6A, FI-20520 Turku, Finland.
Molecules. 2020 Mar 12;25(6):1293. doi: 10.3390/molecules25061293.
Two members of the copper-containing amine oxidase family are physiologically important proteins: (1) Diamine oxidase (hDAO; AOC1) with a preference for diamines is involved in degradation of histamine and (2) Vascular adhesion protein-1 (hVAP-1; AOC3) with a preference for monoamines is a multifunctional cell-surface receptor and an enzyme. hVAP-1-targeted inhibitors are designed to treat inflammatory diseases and cancer, whereas the off-target binding of the designed inhibitors to hDAO might result in adverse drug reactions. The X-ray structures for both human enzymes are solved and provide the basis for computer-aided inhibitor design, which has been reported by several research groups. Although the putative off-target effect of hDAO is less studied, computational methods could be easily utilized to avoid the binding of VAP-1-targeted inhibitors to hDAO. The choice of the model organism for preclinical testing of hVAP-1 inhibitors is not either trivial due to species-specific binding properties of designed inhibitors and different repertoire of copper-containing amine oxidase family members in mammalian species. Thus, the facts that should be considered in hVAP-1-targeted inhibitor design are discussed in light of the applied structural bioinformatics and structural biology approaches.
(1) 具有二胺偏好的二胺氧化酶(hDAO;AOC1)参与组胺的降解,以及 (2) 具有单胺偏好的血管黏附蛋白-1(hVAP-1;AOC3)是一种多功能细胞表面受体和酶。针对 hVAP-1 的抑制剂被设计用于治疗炎症性疾病和癌症,而设计抑制剂与 hDAO 的非靶标结合可能导致不良反应。两种人类酶的 X 射线结构已被解决,为计算机辅助抑制剂设计提供了基础,这已被几个研究小组报道。尽管 hDAO 的潜在非靶标效应研究较少,但可以轻松利用计算方法避免 VAP-1 靶向抑制剂与 hDAO 的结合。由于设计抑制剂的物种特异性结合特性和哺乳动物物种中铜胺氧化酶家族成员的不同 repertoire,选择 hVAP-1 抑制剂的临床前测试的模式生物也不是一件简单的事情。因此,根据应用结构生物信息学和结构生物学方法,讨论了在 hVAP-1 靶向抑制剂设计中应考虑的事实。