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EnglishHerein, we report for the first time that nematic liquid-crystalline environments drive the reversible self-aggregation of an enantiopure -pentapeptide into oligomers with a well-defined structure. The peptide contains four (1S,2S)-2-aminocyclopentane carboxylic acid (ACPC) residues and the paramagnetic -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.
| Titolo: | Self-Association of an Enantiopure β-Pentapeptide in Nematic Liquid Crystals | |
| Autori: | ||
| Data di pubblicazione: | 2013 | |
| Rivista: | ||
| Abstract: | Herein, we report for the first time that nematic liquid-crystalline environments drive the reversible self-aggregation of an enantiopure -pentapeptide into oligomers with a well-defined structure. The peptide contains four (1S,2S)-2-aminocyclopentane carboxylic acid (ACPC) residues and the paramagnetic -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. | |
| Handle: | http://hdl.handle.net/11577/2827136 | |
| Appare nelle tipologie: | 01.01 - Articolo in rivista |
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