表面等离子体共振光谱法在测定淀粉样β蛋白（Abeta）与脂质膜之间的相互作用中的应用

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

作者信息

Hou Xu, Small David H, Aguilar Marie-Isabel

机构信息

Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.

出版信息

Methods Mol Biol. 2010;627:225-35. doi: 10.1007/978-1-60761-670-2_15.

DOI:10.1007/978-1-60761-670-2_15

PMID:20217625

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.

摘要

表面等离子体共振（SPR）光谱正逐渐成为实时测定分子相互作用的一种有用工具。对淀粉样变性分子发病机制的研究表明，质膜在淀粉样蛋白生成以及淀粉样蛋白生成蛋白诱导的细胞毒性中起着重要作用。通过将脂质双层固定在传感器芯片表面，SPR光谱已被用于检测淀粉样蛋白生成蛋白，如β淀粉样蛋白（Aβ）与各种脂质膜的结合，并且它为这些淀粉样蛋白生成蛋白与膜之间的分子相互作用提供了新的见解。在本章中，我们描述了SPR光谱在测定Aβ与脂质膜结合方面的应用。