表面等离子体共振光谱法：研究淀粉样变甲状腺素转运蛋白膜结合的新线索。

Surface plasmon resonance spectroscopy: a new lead in studying the membrane binding of amyloidogenic transthyretin.

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, VIC, Australia.

出版信息

Methods Mol Biol. 2011;752:215-28. doi: 10.1007/978-1-60327-223-0_14.

DOI:10.1007/978-1-60327-223-0_14

PMID:21713640

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.

摘要

表面等离子体共振（SPR）利用SPR的光学原理实时测量传感器芯片表面质量的变化。现已开发出表面化学方法，可实现脂质双层的固定化并实时测定蛋白质与膜的相互作用。在过去十年中，已证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发挥重要作用。SPR为研究淀粉样蛋白生成蛋白的膜结合提供了理想的方法。在本章中，我们描述了SPR在研究淀粉样前体蛋白转甲状腺素蛋白与质膜和人工脂质双层结合方面的应用。