Abstract:
: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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Willemsen OH,Snel MM,Cambi A,Greve J,De Grooth BG,Figdor CGdoi
10.1016/S0006-3495(00)76559-3subject
Has Abstractpub_date
2000-12-01 00:00:00pages
3267-81issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(00)76559-3journal_volume
79pub_type
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