Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy.
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.
Thormann
Esben
E
MEMPHYS-Center for Biomembrane Physics, Department of Physics and Chemistry, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
Simonsen
Adam C
AC
Nielsen
Lars K
LK
Mouritsen
Ole G
OG
D050260:Carbohydrate Metabolism / Q000502:physiology; D002241:Carbohydrates / Q000737:chemistry; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure*; D008024:Ligands; D018625:Microscopy, Atomic Force; D008856:Microscopy, Fluorescence / Q000379:methods*; D008954:Models, Biological; D010713:Phosphatidylcholines / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary / Q000502:physiology; D037663:Pulmonary Surfactant-Associated Protein D / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*
D002241:Carbohydrates; D008024:Ligands; D010713:Phosphatidylcholines; D037663:Pulmonary Surfactant-Associated Protein D; D011956:Receptors, Cell Surface; C017251:1,2-oleoylphosphatidylcholine