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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Self-association of an enantiopure β-pentapeptide in nematic liquid crystals
Marco Bortolus1, Karen Wright, Antonio Toffoletti
1Department of Chemical Sciences, University of Padova, 35131 Padova (Italy), Fax: (+39) 049-827-5050.
Abstract:
Herein, we report for the first time that nematic liquid-crystalline environments drive the reversible self-aggregation of an enantiopure β-pentapeptide into oligomers with a well-defined structure. The peptide contains four (1S,2S)-2-aminocyclopentane carboxylic acid (ACPC) residues and the paramagnetic β-amino acid (3R,4R)-4-amino-1-oxyl-2,2,5,5-tetramethylpyrrolidine-3-carboxylic acid (POAC). The structure of the oligomers was investigated by electron paramagnetic resonance (EPR) spectroscopy, which allowed us to obtain the intermonomer distance distribution in the aggregates as a function of peptide concentration in two nematic liquid crystals, E7 and ZLI-4792. The aggregates were modeled on the basis of the EPR data, and their orientation and order in the nematic phase were studied by the surface tensor method.
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