Biomolecular Interactions Measured by Atomic Force Microscopy

O.H. Willemsen, M.M.E. Snel, A. Cambi, J. Greve, B.G. de Grooth, C.G. Figdor

    Research output: Contribution to journalArticleAcademicpeer-review

    215 Citations (Scopus)
    43 Downloads (Pure)


    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.
    Original languageEnglish
    Pages (from-to)3267-3281
    Number of pages5
    JournalBiophysical journal
    Issue number6
    Publication statusPublished - 2000


    Dive into the research topics of 'Biomolecular Interactions Measured by Atomic Force Microscopy'. Together they form a unique fingerprint.

    Cite this