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Self‐Association of an Enantiopure β‐Pentapeptide in Nematic Liquid Crystals
Author(s) -
Bortolus Marco,
Wright Karen,
Toffoletti Antonio,
Toniolo Claudio,
Maniero Anna Lisa
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201303000
Subject(s) - liquid crystal , pentapeptide repeat , electron paramagnetic resonance , enantiopure drug , paramagnetism , peptide , crystallography , materials science , chemistry , carboxylic acid , organic chemistry , nuclear magnetic resonance , condensed matter physics , physics , biochemistry , optoelectronics , enantioselective synthesis , catalysis
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 (1 S ,2 S )‐2‐aminocyclopentane carboxylic acid (ACPC) residues and the paramagnetic β‐amino acid (3 R ,4 R )‐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.