To establish the mechanism that accounted for the relatively higher potential binding affinity of 1,2BAB-2-MPE, and FGI-103, a molecular visualization of the binding interactions of each compound was determined using the Discovery Studio software (Biovia, 2017). As shown inFigure 2A, the potential binding of 1,2BAB-2-MPE is mediated by high-affinity interactions with hydrogen bond interaction with LYS237 and π-alkyl interactions with LYS241, TYR240, and ALA210. In addition to observed van der Waals interactions, these peculiar interactions collectively anchored 1,2BAB-2-MPE to the binding pocket, favoring stability and high-affinity binding.