Semi-automatized processing of AFM force-spectroscopy data

被引:24
作者
Gergely, C
Senger, B
Voegel, JC
Hörber, JKH
Schaaf, P
Hemmerlé, J
机构
[1] Univ Strasbourg 1, Federat Rech Odontol, INSERM, Unite 424, F-67085 Strasbourg, France
[2] European Mol Biol Lab, D-69012 Heidelberg, Germany
[3] Univ Strasbourg 1, CNRS, Inst Charles Sadron, F-67083 Strasbourg, France
关键词
non-specific adhesion; proteins; force assessments;
D O I
10.1016/S0304-3991(00)00063-2
中图分类号
TH742 [显微镜];
学科分类号
摘要
Atomic force microscopy operated in the force-spectroscopy mode is now a widespread technique, often used to investigate ligand-receptor interactions with the goal of measuring forces at the individual molecule level. However, in an experiment, the simultaneous interaction of several ligand/receptor pairs cannot he excluded. This may product complicated force curves, although unambiguous ruptures are sometimes observed. In the case of the non-specific adhesion of molecules. such as fibrinogen. to a surface, it is usually difficult to identify the real events on the force curves. This can render the application of fixed rules uneasy and in addition can introduce some degree of arbitrariness if the analysis has to be performed by hand. In the present paper a computer algorithm, aimed at speeding up the processing, and at applying selection rules in a reproducible manner, is proposed. It is applied to force recordings performed at various retraction velocities. thus various loading rates. The influence on the evaluation of the rupture forces of the different parameters that can be set by the operator is discussed. (C) 2001 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:67 / 78
页数:12
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