Programming the internal structure and stability of helical pores self-assembled from dendritic dipeptides via the protective groups of the peptide.
The synthesis of dendritic dipeptides (4-3,4-3,5)12G2-CH2-X-L-Tyr-L-Ala-OMe with X = Boc, Moc, and Ac; their self-assembly in bulk and in solution; and the structural and retrostructural analysis of their supramolecular helical porous assemblies are reported. The dimensions, structure, internal order, thermal stability of the supramolecular helical pores, and conformations of the dendron and supramolecular dendrimer are programmed by the nature of the protective groups of the dipeptide. The ability of the protective groups to program the structure of the helical pore reveals the simplest design strategy that complements the more complex strategies based on the architecture of the dendron, the stereochemistry, and the structure of the dipeptide.
Percec
Virgil
V
Roy & 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
Ilies
Monica
M
Sienkowska
Monika J
MJ
Heiney
Paul A
PA
D000409:Alanine / Q000737:chemistry; D002942:Circular Dichroism; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry*; D005563:Formic Acid Esters / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D014443:Tyrosine / Q000737:chemistry
D004151:Dipeptides; D005563:Formic Acid Esters; D010455:Peptides; C000345:t-butyloxycarbonyl group; D014443:Tyrosine; D000409:Alanine