Helical pores self-assembled from homochiral dendritic dipeptides based on L-Tyr and nonpolar alpha-amino acids.
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 structural and retrostructural analysis of their periodic assemblies were compared to those of the previously reported and currently reinvestigated dendritic dipeptides with X = L-Ala. All dendritic dipeptides containing as X nonpolar alpha-amino acids self-assemble into helical porous columns. The substituent of X programs the structure of the helical pore and the resulting periodic array, in spite of the fact that its molar mass represents only between 0.05 and 4.77% from the molar mass of the dendritic dipeptide. In addition to the various 2-D columnar lattices, the dendritic dipeptides based on L-Ala, L-Leu, and L-Phe self-organize into 3-D hexagonal columnar crystals while those based on L-Val and L-Ile into an unknown columnar crystal. The principles via which the aliphatic and aromatic substituents of X program the structure of the helical pores indicate synthetic pathways to helical pores with bioinspired functions based on artificial nonpolar alpha-amino acids.
Percec
Virgil
V
Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA. percec@sas.upenn.edu
Dulcey
Andrés E
AE
Peterca
Mihai
M
Adelman
Peter
P
Samant
Ritika
R
Balagurusamy
Venkatachalapathy S K
VS
Heiney
Paul A
PA
D000596:Amino Acids / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D004151:Dipeptides / Q000737:chemistry*; D011487:Protein Conformation; D013057:Spectrum Analysis; D014443:Tyrosine / Q000737:chemistry*; D014961:X-Ray Diffraction
D000596:Amino Acids; D004151:Dipeptides; D014443:Tyrosine