Jump to main content
Jump to site search

Issue 45, 2011
Previous Article Next Article

Probing small molecule binding to amyloid fibrils

Author affiliations


Much effort has focussed in recent years on probing the interactions of small molecules with amyloid fibrils and other protein aggregates. Understanding and control of such interactions are important for the development of diagnostic and therapeutic strategies in situations where protein aggregation is associated with disease. In this perspective article we give an overview over the toolbox of biophysical methods for the study of such amyloid-small molecule interactions. We discuss in detail two recently developed techniques within this framework: linear dichroism, a promising extension of the more traditional spectroscopic techniques, and biosensing methods, where surface-bound amyloid fibrils are exposed to solutions of small molecules. Both techniques rely on the measurement of physical properties that are very directly linked to the binding of small molecules to amyloid aggregates and therefore provide an attractive route to probe these important interactions.

Graphical abstract: Probing small molecule binding to amyloid fibrils

Back to tab navigation

Publication details

The article was received on 13 Jul 2011, accepted on 12 Sep 2011 and first published on 17 Oct 2011

Article type: Perspective
DOI: 10.1039/C1CP22283J
Phys. Chem. Chem. Phys., 2011,13, 20044-20052

  •   Request permissions

    Probing small molecule binding to amyloid fibrils

    A. K. Buell, E. K. Esbjörner, P. J. Riss, D. A. White, F. I. Aigbirhio, G. Toth, M. E. Welland, C. M. Dobson and T. P. J. Knowles, Phys. Chem. Chem. Phys., 2011, 13, 20044
    DOI: 10.1039/C1CP22283J

Search articles by author