Single-molecule force spectroscopy: A method for quantitative analysis of ligand-receptor interactions

Alexander Fuhrmann, Robert Ros

Research output: Contribution to journalReview articlepeer-review

36 Scopus citations


The quantitative analysis of molecular interactions is of high interest in medical research. Most methods for the investigation of ligand-receptor complexes deal with huge ensembles of biomolecules, but often neglect interactions with low affinity or small subpopulations with different binding properties. Single-molecule force spectroscopy offers fascinating possibilities for the quantitative analysis of ligand-receptor interactions in a wide affinity range and the sensitivity to detect point mutations. Furthermore, this technique allows one to address questions about the related binding energy landscape. In this article, we introduce single-molecule force spectroscopy with a focus on novel developments in both data analysis and theoretical models for the technique. We also demonstrate two examples of the capabilities of this method.

Original languageEnglish (US)
Pages (from-to)657-666
Number of pages10
Issue number4
StatePublished - Jun 2010


  • Atomic force microscopy
  • Force spectroscopy
  • Ligandreceptor
  • Single molecule

ASJC Scopus subject areas

  • Bioengineering
  • Medicine (miscellaneous)
  • Biomedical Engineering
  • Materials Science(all)


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