These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Ligand-receptor interactions and membrane structure investigated by AFM and time-resolved fluorescence microscopy.
    Author: Thormann E, Simonsen AC, Nielsen LK, Mouritsen OG.
    Journal: J Mol Recognit; 2007; 20(6):554-60. PubMed ID: 17907279.
    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.
    [Abstract] [Full Text] [Related] [New Search]