133301-03-8Relevant articles and documents
Photophysical study of a π-stacked β-sheet nanofibril forming peptide bolaamphiphile hydrogel
Maity, Indrajit,Mukherjee, Tushar K.,Das, Apurba K.
supporting information, p. 376 - 385 (2014/01/06)
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. The Royal Society of Chemistry and the Centre National de la Recherche Scientifique 2014.
Synthesis and binding properties of a macrocyclic peptide receptor
Dowden, James,Edwards, Peter D.,Flack, Stephen S.,Kilburn, Jeremy D.
, p. 79 - 89 (2007/10/03)
Macrocyclic receptor 1 has been synthesised, as a racemate and as a single enantiomer, utilising a Stille coupling for the formation of the biphenyl portion and a macrolactamisation as the final step. The binding properties for the racemic and the homochi
