bis(5-amidino-benzimidazolyl)methanone zinc

Bis(5-amidino-benzimidazolyl)methanone zinc is an experimental small molecule compound in which a zinc ion is chelated by two 5-amidino-benzimidazolyl moieties connected through a methanone (ketone) bridge[1][2][4]. This unique structure enables the compound to act as a potent and selective inhibitor of serine proteases such as trypsin and thrombin by recruiting physiological Zn²⁺ to mediate high-affinity binding at the enzyme active site[7]. The mechanism involves tetrahedral coordination of Zn²⁺ between the benzimidazole nitrogens of the inhibitor and key residues in the protease active site (notably His57 and Ser195)[7]. It has not been approved for any indication or entered clinical trials beyond preclinical/structural studies[1].

Other names

BIS(5-AMIDINO-BENZIMIDAZOLYL)METHANONE ZINC7,17-bis(diaminomethyl)-12-oxo-1??,3??,10,14-tetraaza-2-zincapentacyclo[11.7.0.03,11.0?,?.01?,2?]icosa-1(13),3(11),4(9),5,7,15(20),16,18-octaene-1,3-bis(ylium)