Journal
NEW JOURNAL OF CHEMISTRY
Volume 38, Issue 1, Pages 376-385Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3nj00814b
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Funding
- DST [SR/FT/CS-67/2010]
- CSIR, New Delhi, India [02(0056)/12/EMR-II]
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We describe the state of molecular self-assembly of a peptide based bolaamphiphile molecule using spectroscopic and microscopic techniques. The tryptophan and phenylalanine containing peptide bolaamphiphile forms a hydrogel upon sonication under physiological conditions. Sonication helps to reorient the peptide molecules by providing the required energy for the self-assembly process. The disassembly and self-assembly processes are influenced by various stimuli, including heating cooling and shaking-rest methods. The extensive hydrogen bonding and pi-pi stacking interactions are responsible for the self-assembly process, which is confirmed by FT-IR, temperature dependent NMR and fluorescence spectroscopy studies. FT-IR and powder X-ray diffraction studies reveal that the gelator molecules self-assemble into an antiparallel beta-sheet type structure. The TEM image of the hydrogel shows a welt-defined amyloid-like nanofibrillar structure. The amyloid-like behaviour of the fibril forming peptide bolaamphiphile hydrogel is confirmed by ThT and Congo red binding studies. The effect of concentration, time and temperature on the self-assembly mechanism of the peptide bolaamphiphile hydrogel is investigated by time resolved fluorescence spectroscopy.
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