Inhibition of amyloid β protein fibrillation by polymeric nanoparticles

C. Cabaleiro-Lago, F. Quinlan-Pluck, I. Lynch, K.A. Dawson, S. Lindman, E. Thulin, S. Linse, A.M. Minogue, D.M. Walsh

Research output: Contribution to journalArticlepeer-review

482 Citations (Scopus)


Copolymeric NiPAM:BAM nanoparticles of varying hydrophobicity were found to retard fibrillation of the Alzheimer's disease-associated amyloid β protein (Aβ). We found that these nanoparticles affect mainly the nucleation step of Aβ fibrillation. The elongation step is largely unaffected by the particles, and once the Aβ is nucleated, the fibrillation process occurs with the same rate as in the absence of nanoparticles. The extension of the lag phase for fibrillation of Aβ is strongly dependent on both the amount and surface character of the nanoparticles. Surface plasmon resonance studies show that Aβ binds to the nanoparticles and provide rate and equilibrium constants for the interaction. Numerical analysis of the kinetic data for fibrillation suggests that binding of monomeric Aβ and prefibrillar oligomers to the nanoparticles prevents fibrillation. Moreover, we find that fibrillation of Aβ initiated in the absence of nanoparticles can be reversed by addition of nanoparticles up to a particular time point before mature fibrils appear.
Original languageEnglish
Pages (from-to)15437-15443
Number of pages7
JournalJournal of the American Chemical Society
Issue number46
Publication statusPublished - 19 Nov 2008

Bibliographical note

MEDLINE® is the source for the MeSH terms of this document.


Dive into the research topics of 'Inhibition of amyloid β protein fibrillation by polymeric nanoparticles'. Together they form a unique fingerprint.

Cite this