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Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy
MEMPHYS - Center for Biomembrane Physics, Department of Physics and Chemistry, University of Southern Denmark.
2007 (English)In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 20, no 6, 554-560 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 20, no 6, 554-560 p.
Keyword [en]
Atomic force microscopy, Force spectroscopy, Lateral membrane structure, Ligand-receptor interaction, Phospholipase A2, Single molecules, Surfactant protein D
National Category
Natural Sciences
URN: urn:nbn:se:kth:diva-62273DOI: 10.1002/jmr.850ISI: 000252782400018OAI: diva2:480051
QC 20120119Available from: 2012-01-18 Created: 2012-01-18 Last updated: 2012-01-19Bibliographically approved

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Thormann, Esben
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