Biosensor-based label-free assays of amyloid growth

被引：38

作者：

White, Duncan A. ^{[1
,2
]}

Buell, Alexander K. ^{[1
]}

Dobson, Christopher M. ^{[2
]}

Welland, Mark E. ^{[1
]}

Knowles, Tuomas P. J. ^{[1
]}

机构：

[1] Univ Cambridge, Nanosci Ctr, Cambridge CB3 0FF, England

[2] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

来源：

FEBS LETTERS | 2009年 / 583卷 / 16期

基金：

英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

Amyloid; Protein aggregation; QCM; SPR; QUARTZ-CRYSTAL MICROBALANCE; BETA-PROTEIN AGGREGATION; KINETIC-ANALYSIS; SURFACE-ROUGHNESS; FIBRIL FORMATION; THIOFLAVIN-T; BINDING; ADSORPTION; FREQUENCY; CELLS;

D O I：

10.1016/j.febslet.2009.06.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Uncontrolled fibrous protein aggregation is implicated in a range of aberrant biological phenomena. Much effort has consequently been directed towards establishing quantitative in vitro assays of this process with the aim of probing amyloid growth in molecular detail as well as elucidating the effect of additional species on this reaction. In this paper, we discuss some recent approaches based on label-free technologies focussed on achieving these objectives. Several biosensor techniques have been developed to monitor biomolecular assembly without the requirement for fluorophore marker molecules; in particular quartz crystal microbalance and surface plasmon resonance measurements provide advantageous alternatives to traditional spectroscopic methods and are currently receiving increasing attention in the context of amyloid growth assays. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：2587 / 2592

页数：6

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