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

Esben Thormann, Adam C. Simonsen, Lars K. Nielsen, Ole G. Mouritsen*

*Corresponding author for this work
    18 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    JournalJournal of Molecular Recognition
    Volume20
    Issue number6
    Pages (from-to)554-560
    Number of pages7
    ISSN0952-3499
    DOIs
    Publication statusPublished - 1 Nov 2007

    Keywords

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

    Fingerprint

    Dive into the research topics of 'Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy'. Together they form a unique fingerprint.

    Cite this