Amyloid beta peptides inside a reconstituted cell-like liposomal system: aggregation, FRET, fluorescence oscillations and solvation dynamics.
Phys Chem Chem Phys
; 18(44): 30444-30451, 2016 Nov 09.
Article
em En
| MEDLINE
| ID: mdl-27781218
ABSTRACT
Aggregations of amyloid-beta (Aß) peptides were studied inside a reconstituted cell like liposomal system using time-resolved confocal microscopy. Fluorescence correlation spectroscopy (FCS) and confocal images indicate that Aß 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 Aß peptide) to TRITC (tetramethylrhodamine isothiocyanate) covalently attached to a DHPE lipid present in the bilayer, reveals intermittent oscillations in the time scale of â¼0.5 s. This is attributed to the structural fluctuations of the membrane of the liposome. The solvation dynamics of Aß in monomer and in oligomeric state is studied by monitoring the emission of HiLyte Fluor 488. The solvation dynamics of the Aß monomer is similar to that of oligomeric aggregates in the liposome.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos beta-Amiloides
/
Lipossomos
Idioma:
En
Revista:
Phys Chem Chem Phys
Assunto da revista:
BIOFISICA
/
QUIMICA
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Índia