Issue 44, 2016

Amyloid beta peptides inside a reconstituted cell-like liposomal system: aggregation, FRET, fluorescence oscillations and solvation dynamics

Abstract

Aggregations of amyloid-beta (Aβ) peptides were studied inside a reconstituted cell like liposomal system using time-resolved confocal microscopy. Fluorescence correlation spectroscopy (FCS) and confocal images indicate that Aβ forms a very large aggregate in bulk and more efficiently, in the bilayer region of the liposome, respectively. The aggregates formed inside the liposome gradually migrate out to bulk water. FRET, from HiLyte Fluor 488 (covalently attached to an Aβ peptide) to TRITC (tetramethylrhodamine isothiocyanate) covalently attached to a DHPE lipid present in the bilayer, reveals intermittent oscillations in the time scale of ∼0.5 s. This is attributed to the structural fluctuations of the membrane of the liposome. The solvation dynamics of Aβ in monomer and in oligomeric state is studied by monitoring the emission of HiLyte Fluor 488. The solvation dynamics of the Aβ monomer is similar to that of oligomeric aggregates in the liposome.

Graphical abstract: Amyloid beta peptides inside a reconstituted cell-like liposomal system: aggregation, FRET, fluorescence oscillations and solvation dynamics

Supplementary files

Article information

Article type
Paper
Submitted
06 Sep 2016
Accepted
13 Oct 2016
First published
13 Oct 2016

Phys. Chem. Chem. Phys., 2016,18, 30444-30451

Amyloid beta peptides inside a reconstituted cell-like liposomal system: aggregation, FRET, fluorescence oscillations and solvation dynamics

S. Nandi, P. Mondal, R. Chowdhury, A. Saha, S. Ghosh and K. Bhattacharyya, Phys. Chem. Chem. Phys., 2016, 18, 30444 DOI: 10.1039/C6CP06143E

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