Single-molecule force spectroscopy

A method for quantitative analysis of ligand-receptor interactions

Alexander Fuhrmann, Robert Ros

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

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
JournalNanomedicine
Volume5
Issue number4
DOIs
StatePublished - Jun 2010

Fingerprint

quantitative analysis
ligand
spectroscopy
Ligands
Psychological Techniques
Spectroscopy
Molecules
Molecular interactions
Biomolecules
interaction
Binding energy
subpopulation
Chemical analysis
Point Mutation
Biomedical Research
mutation
Theoretical Models
medical research
neglect
data analysis

Keywords

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

ASJC Scopus subject areas

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

Cite this

Single-molecule force spectroscopy : A method for quantitative analysis of ligand-receptor interactions. / Fuhrmann, Alexander; Ros, Robert.

In: Nanomedicine, Vol. 5, No. 4, 06.2010, p. 657-666.

Research output: Contribution to journalArticle

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