Photophysical study of a π-stacked β-sheet nanofibril forming peptide bolaamphiphile hydrogel

Indrajit Maity, Tushar K. Mukherjee, Apurba K. Das

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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 π-π 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 β-sheet type structure. The TEM image of the hydrogel shows a well-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.

Original languageEnglish
Pages (from-to)376-385
Number of pages10
JournalNew Journal of Chemistry
Volume38
Issue number1
DOIs
StatePublished - 1 Jan 2014
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry (all)
  • Materials Chemistry

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