Probing beta amyloid aggregation using fluorescence anisotropy: experiments and simulation

Onorio Mancini, Thorben Wellbrock, Olaf J. Rolinski, Karina Kubiak-Ossowska, Paul A. Mulheran

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)
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The aggregation of beta amyloid (Ab) protein is associated with the development of Alzheimer's disease. In this work we monitor Ab aggregation using fluorescence anisotropy, a technique that provides information on the rotational diffusion of the fluorescing tyrosine (Tyr) side chains. We also perform Monte Carlo (MC) and fully atomistic Molecular Dynamics (MD) simulations to interpret the experiments. The experimental results show that there are two different rotational timescales contributing to the anisotropy. Our MC simulation captures this behaviour in a coarse-scale manner, and, more importantly, shows that the Tyr side chains must have their movements restricted in order to reproduce the anisotropy. The MD simulations provide a molecular scale view, and indeed show that aggregation restricts the Try side chains to yield anisotropy in line with the experimental results. This combination of experiment and simulation therefore provides a unique insight into the aggregation process, and we suggest how this approach might be used to gain further information on aggregating protein systems.
Original languageEnglish
Pages (from-to)4216-4225
Number of pages10
JournalPhysical Chemistry Chemical Physics
Issue number6
Publication statusPublished - 16 Jan 2018


  • Alzheimer's disease
  • beta amyloid
  • anisotropy
  • protein systems


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