Surface plasmon resonance spectroscopy in determination of the interactions between amyloid beta proteins (Abeta) and lipid membranes.

Abstract

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.

• Authors: Xu Hou, David H Small, Marie-Isabel Aguilar
• Journal: Methods in molecular biology (Clifton, N.J.) (Methods Mol Biol) Vol. 627 Pg. 225-35 ( 2010) ISSN: 1940-6029 [Electronic] United States
• PMID: 20217625 (Publication Type: Journal Article)

Chemical References

• Amyloid beta-Peptides
• Membranes, Artificial
• Phospholipids

Topics

• Amyloid beta-Peptides (metabolism)
• Animals
• Cell Membrane (metabolism)
• Lipid Metabolism
• Membranes, Artificial
• Muscle, Smooth, Vascular (cytology)
• Phospholipids (metabolism)
• Protein Binding
• Surface Plasmon Resonance (methods)