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Ligand–receptor interactions and membrane structure investigated by AFM and time‐resolved fluorescence microscopy
Author(s) -
Thormann Esben,
Simonsen Adam C.,
Nielsen Lars K.,
Mouritsen Ole G.
Publication year - 2007
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.850
Subject(s) - atomic force microscopy , biophysics , chemistry , liposome , fluorescence microscope , microscopy , force spectroscopy , lipid bilayer , membrane , nanotechnology , fluorescence , ligand (biochemistry) , pulmonary surfactant , receptor , materials science , biochemistry , biology , optics , physics
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. Copyright © 2007 John Wiley & Sons, Ltd.