Oligo-benzamide-based peptide mimicking tools for modulating biology.

The oligo-benzamide scaffold is a rigid organic framework that can hold 2-3 functional groups as O-alkyl substituents on its benzamide units, mirroring their natural arrangement in an α-helix. Oligo-benzamides demonstrated outstanding α-helix mimicry and can be readily synthesized by following high yielding and iterative reaction steps in both solution-phase and solid-phase. A number of oligo-benzamides have been designed to emulate α-helical peptide segments in biologically active proteins and showed strong protein binding, in turn effectively disrupting protein-protein interactions in vitro and in vivo. In this chapter, the design of oligo-benzamides for mimicking α-helices, efficient synthetic routes for producing them, and their biomedical studies showing remarkable potency in inhibiting protein functions are discussed.

1,1'-Methyl-enebis{4-[(E)-2-(pyridin-4-yl)ethen-yl]pyridinium} dibromide dihydrate.

The chevron-shaped cations of the title hydrated salt, C25H22N4 2+·2Br-·2H2O, are arranged in back-to-back alternating directions to form a zigzag ribbon propagating along the [010] direction. Inter-molecular inter-actions comprising these ribbons are π-π inter-actions between the pyridinium and adjacent pyridyl rings, as well as O-H⋯O hydrogen bonding between water molecules and two adjacent pyridyl N atoms. Half of the cation is generated by the mirror plane. The water O atoms, the central C atom and one Br atom are located on this mirror plane while the other Br atom is on a twofold screw axis.