1504562-54-2Relevant academic research and scientific papers
Self-programmed nanovesicle to nanofiber transformation of a dipeptide appended bolaamphiphile and its dose dependent cytotoxic behaviour
Maity, Indrajit,Parmar, Hamendra S.,Rasale, Dnyaneshwar B.,Das, Apurba K.
, p. 5272 - 5279 (2014)
Nanostructural transition of a small peptide bolaamphiphile via molecular self-assembly is a challenging task. Here, we report the self-programmed morphological transformation from nanovesicles to nanofibers of a smart peptide bolaamphiphile in its self-assembling hydrogel state. The nanostructural transition occurs based on the structural continuity of the β-sheet structures. Spectroscopic studies confirmed the different molecular arrangements of the two different nanostructures. Furthermore, the smart bolaamphiphile shows a dose-dependent cytotoxicity and cell-proliferation behaviour. This journal is the Partner Organisations 2014.
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.
