title: Probing small molecule binding to amyloid fibrils.
abstract: 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.
authors: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors: Alexander K
authors: AK
authors: Buell
authors: Elin K
authors: EK
authors: Esbjörner
authors: Patrick J
authors: PJ
authors: Riss
authors: Duncan A
authors: DA
authors: White
authors: Franklin I
authors: FI
authors: Aigbirhio
authors: Gergely
authors: G
authors: Toth
authors: Mark E
authors: ME
authors: Welland
authors: Christopher M
authors: CM
authors: Dobson
authors: Tuomas P J
authors: TP
authors: Knowles
mesh_terms: D000544:Alzheimer Disease / Q000000981:diagnostic imaging; D000682:Amyloid / Q000032:analysis* / Q000378:metabolism*; D000818:Animals; D006801:Humans; D011485:Protein Binding; D058525:Quartz Crystal Microbalance Techniques / Q000379:methods; D011877:Radionuclide Imaging; D054852:Small Molecule Libraries / Q000494:pharmacology*; D013057:Spectrum Analysis / Q000379:methods
chemical_list: D000682:Amyloid; D054852:Small Molecule Libraries