| Abstract
| - The synthesis of dendritic dipeptides (4-3,4-3,5)12G2-CH2-Boc-l-Tyr-X-OMe where X = Gly,l-Val, l-Leu, l-Ile, l-Phe, and l-Pro is reported. Their self-assembly in bulk and in solution and the structuraland retrostructural analysis of their periodic assemblies were compared to those of the previously reportedand currently reinvestigated dendritic dipeptides with X = l-Ala. All dendritic dipeptides containing as Xnonpolar α-amino acids self-assemble into helical porous columns. The substituent of X programs thestructure of the helical pore and the resulting periodic array, in spite of the fact that its molar mass representsonly between 0.05 and 4.77% from the molar mass of the dendritic dipeptide. In addition to the various2-D columnar lattices, the dendritic dipeptides based on l-Ala, l-Leu, and l-Phe self-organize into 3-Dhexagonal columnar crystals while those based on l-Val and l-Ile into an unknown columnar crystal. Theprinciples via which the aliphatic and aromatic substituents of X program the structure of the helical poresindicate synthetic pathways to helical pores with bioinspired functions based on artificial nonpolar α-aminoacids.
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