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

Thormann, Esben (author)
MEMPHYS - Center for Biomembrane Physics, Department of Physics and Chemistry, University of Southern Denmark
Simonsen, Adam C. (author)
Nielsen, Lars K. (author)
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Mouritsen, Ole G. (author)
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 (creator_code:org_t)
2007
2007
English.
In: Journal of Molecular Recognition. - : Wiley. - 0952-3499 .- 1099-1352. ; 20:6, s. 554-560
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

Atomic force microscopy
Force spectroscopy
Lateral membrane structure
Ligand-receptor interaction
Phospholipase A2
Single molecules
Surfactant protein D

Publication and Content Type

ref (subject category)
art (subject category)

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