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Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin
Citation
Hou, X and Small, DH and Aguilar, MI, Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin, Methods in Molecular Biology, 752 pp. 215-228. ISSN 1064-3745 (2011) [Refereed Article]
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Copyright Statement
Copyright 2011 Springer Science+Business Media, LLC
DOI: doi:10.1007/978-1-60327-223-0_14
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.
Item Details
| Item Type: | Refereed Article |
|---|---|
| Keywords: | Amyloid; Transthyretin; Surface plasmon resonance; BIACORE biosensor; Plasma membrane; Lipid vesicle; Binding; Aqueous two-phase partition sytem |
| Research Division: | Biomedical and Clinical Sciences |
| Research Group: | Neurosciences |
| Research Field: | Neurosciences not elsewhere classified |
| Objective Division: | Health |
| Objective Group: | Clinical health |
| Objective Field: | Clinical health not elsewhere classified |
| UTAS Author: | Small, DH (Professor David Small) |
| ID Code: | 76273 |
| Year Published: | 2011 |
| Deposited By: | Menzies Institute for Medical Research |
| Deposited On: | 2012-03-02 |
| Last Modified: | 2017-11-06 |
| Downloads: | 0 |
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