Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy
Research output: Contribution to journal › Journal article › Research › peer-review
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.
|Journal||Journal of Molecular Recognition|
|Number of pages||7|
|Publication status||Published - 1 Nov 2007|
- Atomic force microscopy, Force spectroscopy, Lateral membrane structure, Ligand-receptor interaction, Phospholipase A, Single molecules, Surfactant protein D