Abstract
Surface plasmon resonance (SPR) employs the optical principle of SPR to measure changes in mass on a sensor chip surface in real time. Surface chemistry has been developed which enables the immoblization of lipid bilayers and determination of protein-membrane interactions in real time. In the last decade, the plasma membrane has been demonstrated to play an important role in amyloidogenesis and cytotoxicity induced by amyloidogenic proteins. SPR provides an ideal way to study the membrane binding of amyloidogenic proteins. In this chapter, we describe the application of SPR to the study of amyloidogenic transthyretin binding to the plasma membrane and artificial lipid bilayers.
| Original language | English |
|---|---|
| Title of host publication | Protein Folding, Misfolding and Disease - Methods and Protocols |
| Editors | Andrew F Hill, Kevin J Barnham, Stehen P Bottomley, Roberto Cappai |
| Place of Publication | USA |
| Publisher | Humana Press |
| Pages | 215 - 228 |
| Number of pages | 14 |
| Edition | 1st |
| ISBN (Print) | 9781603272216 |
| DOIs | |
| Publication status | Published - 2011 |
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