Biomolecular interactions measured by atomic force microscopy.
Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitative. At the same time, theories have been developed to describe and understand the dynamics of the unbinding process and experimental techniques have been refined to verify this theory. In addition, the detection of molecular recognition forces has been exploited to map and image the location of binding sites. In this review we discuss the important contributions that have led to the development of this field. In addition, we emphasize the potential of chemically well-defined surface modification techniques to further improve reproducible measurements by AFM. This increased reproducibility will pave the way for a better understanding of molecular interactions in cell biology.
Willemsen
O H
OH
Department of Applied Physics, Biophysical Techniques Group, University of Twente, Enschede, The Netherlands.
Snel
M M
MM
Cambi
A
A
Greve
J
J
De Grooth
B G
BG
Figdor
C G
CG
D001703:Biophysics / Q000379:methods*; D018625:Microscopy, Atomic Force / Q000379:methods*; D011506:Proteins / Q000737:chemistry*
D011506:Proteins