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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:Medical and Health Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Neurodegenerative Disorders Related to Ageing
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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