Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy

Research output: Contribution to journalJournal articleResearchpeer-review

  • Esben Thormann
  • Adam C. Simonsen
  • Lars K. Nielsen
  • Ole G. Mouritsen

The atomic force microscope (AFM) and the associated dynamic force spectroscopy technique have been exploited to quantitatively assess the interaction between proteins and their binding to specific ligands and membrane surfaces. In particular, we have studied the specific interaction between lung surfactant protein D and various carbohydrates. In addition, we have used scanning AFM and time-resolved fluorescence microscopy to image the lateral structure of different lipid bilayers and their morphological changes as a function of time. The various systems studied illustrate the potential of modern AFM techniques for application to biomedical research, specifically within immunology and liposome-based drug delivery.

Original languageEnglish
JournalJournal of Molecular Recognition
Issue number6
Pages (from-to)554-560
Number of pages7
Publication statusPublished - 2007
Externally publishedYes
EventAFM BioMed 2007, Atomic force microscopy in life sciences and medicine - Barcelona, Spain
Duration: 19 Apr 200721 Apr 2007


ConferenceAFM BioMed 2007, Atomic force microscopy in life sciences and medicine

    Research areas

  • Atomic force microscopy, Force spectroscopy, Lateral membrane structure, Ligand-receptor interaction, Phospholipase A, Single molecules, Surfactant protein D

ID: 230977523