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Updated: Jul 12, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Programming the internal structure and stability of helical pores self-assembled from dendritic dipeptides via the
Virgil Percec1, Andrés E Dulcey, Mihai Peterca
1Roy & Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, USA. percec@sas.upenn.edu
Abstract:
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.
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