The dynamic nature of amyloid beta (1-40) aggregation

Alik Belitzky, Naomi Melamed-Book, Aryeh Weiss, Uri Raviv

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

In this paper, we characterize the dynamic nature of the full amyloid beta (1-40) (Aβ (1-40)) aggregates. We labeled the peptide with either 5-carboxytetramethylrhodamine (TAMRA) or with fluorescein-isothiocyanate (FITC). The labeled peptides were mixed after separate fibrillization, and the dynamic changes in the structure of the fibrils were imaged using confocal microscopy. Fluorescence resonance energy transfer (FRET) measurements showed that the Aβ (1-40) peptides detach from and reattach to the fibrils in a biologically relevant timescale (days). With time, the two peptides mix at the molecular level. This process is concentration dependent and occurs primarily in the external parts of the aggregates with a half time between 4 and 7 days. This study shows that the combination of confocal microscopy and FRET analysis is a facile method for studying dynamic processes in supra-molecular aggregates.

Original languageEnglish
Pages (from-to)13809-13814
Number of pages6
JournalPhysical Chemistry Chemical Physics
Volume13
Issue number30
DOIs
StatePublished - 14 Aug 2011

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