Surface plasmon resonance spectroscopy in determination of the interactions between amyloid beta proteins (Abeta) and lipid membranes.
Surface plasmon resonance (SPR) spectroscopy is emerging as a useful tool for determination of molecular interactions in real time. Studies on the molecular pathogenesis of amyloidoses have shown that the plasma membrane plays an important role in amyloidogenesis and cytotoxicity induced by amyloidogenic proteins. By immobilizing lipid bilayers on a sensor chip surface, SPR spectroscopy has been employed to examine the binding of amyloidogenic proteins, such as amyloid beta protein (Abeta), to a variety of lipid membranes, and it provided new insights into the molecular interactions between these amyloidogenic proteins and membranes. In this chapter, we describe the application of SPR spectroscopy to the determination of the binding of Abeta to lipid membranes.
Hou
Xu
X
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
Small
David H
DH
Aguilar
Marie-Isabel
MI
D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D050356:Lipid Metabolism; D008567:Membranes, Artificial; D009131:Muscle, Smooth, Vascular / Q000166:cytology; D010743:Phospholipids / Q000378:metabolism; D011485:Protein Binding; D020349:Surface Plasmon Resonance / Q000379:methods*
D016229:Amyloid beta-Peptides; D008567:Membranes, Artificial; D010743:Phospholipids