Vascular adhesion protein-1 (VAP-1), also known as plasma amine oxidase or semicarbazide-sensitive amine oxidase, is an enzyme that degrades primary amines to aldehydes with the formation of hydrogen peroxide and ammonia. Among others, it plays a role in inflammatory processes as it can mediate the migration of leukocytes from the blood to the inflamed tissue. We prepared a series of ω-(5-phenyl-2H-tetrazol-2-yl)alkyl-substituted glycine amides and related compounds and tested them for inhibition of purified bovine plasma VAP-1. Compounds with submicromolar activity were obtained. Studies on the mechanism of action revealed that the glycine amides are substrate inhibitors, i.e., they are also converted to an aldehyde derivative. However, the reaction proceeds much more slowly than that of the substrate used in the assay, whose conversion is thus blocked. Examination of the selectivity of the synthesized glycine amides with respect to other amine oxidases showed that they inhibited diamine oxidase, which is structurally related to VAP-1, but only to a much lesser extent. In contrast, the activity of monoamine oxidase A and B was not affected. Selected compounds also inhibited VAP-1 in human plasma. The IC₅₀ values measured were higher than those determined with the bovine enzyme. However, the structure–activity relationships obtained with the glycine amides were similar for both enzymes.

血管粘附蛋白-1 (VAP-1)，也称为血浆胺氧化酶或氨基脲敏感胺氧化酶，是一种将伯胺降解为醛并形成过氧化氢和氨的酶。其中，它在炎症过程中发挥作用，因为它可以介导白细胞从血液迁移到发炎组织。我们制备了一系列ω-(5-苯基-2H-四唑-2-基)烷基取代的甘氨酸酰胺及相关化合物，并测试了它们对纯化牛血浆VAP-1的抑制作用。获得了具有亚微摩尔活性的化合物。作用机制的研究表明，甘氨酸酰胺是底物抑制剂，即它们也会转化为醛衍生物。然而，反应进行得比测定中使用的底物慢得多，因此底物的转化被阻止。对合成的甘氨酸酰胺相对于其他胺氧化酶的选择性的检查表明，它们抑制二胺氧化酶，其结构与 VAP-1 相关，但程度要小得多。相反，单胺氧化酶A和B的活性不受影响。选定的化合物还抑制人血浆中的 VAP-1。测量的IC ₅₀值高于用牛酶测定的值。然而，两种酶的甘氨酸酰胺的结构-活性关系相似。