Nonspecific interactions in AFM force spectroscopy measurements

被引:22
|
作者
Celik, Emrah [1 ]
Moy, Vincent T. [1 ]
机构
[1] Univ Miami, Dept Physiol & Biophys, Sch Med, Miami, FL 33136 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
atomic force microscopy; nonspecific adhesion; protein adsorption; force spectroscopy; MOLECULAR RECOGNITION; PROTEIN INTERACTIONS; ADHESION FORCES; DNA; ATTACHMENT;
D O I
10.1002/jmr.2152
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
Sample-probe contact duration (dwell time) and loading force are two important parameters for the atomic force microscopy (AFM) force spectroscopy measurements of ligandreceptor interaction. A prolonged contact time may be required to initiate ligandreceptor binding as a result of slow on-rate kinetics or low reactant density. In general, increasing contact duration promotes nonspecific interactions between the substrate and the functionalized cantilever and, thus, masking the detection of the specific interactions. To reduce the nonspecific interactions in AFM force measurements requiring extended substrate-probe contact, we investigated the interaction of bovine serum albumin (BSA)-functionalized cantilever with BSA-coated glass, polyethylene glycol (PEG)-functionalized glass, Pluronic-treated Petri dishes and agarose beads. The frequency of nonspecific interaction between the BSA-functionalized cantilever and the different samples increased with loading force and dwell time. This increase in nonspecific adhesion can be attributed to the interaction mediated by forced unfolding of BSA. By reducing the loading force, the contact duration of the AFM probe with an agarose bead can be extended to a few minutes without nonspecific adhesion. Copyright (C) 2011 John Wiley & Sons, Ltd.
引用
收藏
页码:53 / 56
页数:4
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