Figure:2 Showing the 3D representation of the complex between MARV VP35 and FGI-103. Also showing is the residue interaction profile that mediates the MARV VP35-FGI-103. 2B) Showing the 3D representation of the complex between MARV VP35 and 1,2-1,2BAB-2-MPE. Also showing is the residue interaction profile that mediates the MARV VP35-1,2BAB-2-MPE.
The stronger affinity binding of FGI-103 as evidenced by the highest negative docking score of -4.1kcal/mol was mediated by two strong conventional hydrogen bond interactions with VAL283, and LYS237, a π-alkyl interaction with ILE284 in addition to van der Waals interactions with PRO282 and GLN233. As shown in Figure 2 , the residue LYS237 was observed to engage in conventional hydrogen bond interaction with 1,2BAB-2-MPE and FGI-103, suggesting its cruciality to the therapeutic modulation of MARV VP35 and could therefore guide the future design of novel MARV VP35 inhibitors.