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

Esben Thormann, Adam Cohen Simonsen, Lars Kildemark Nielsen, Ole G. Mouritsen

Research output: Contribution to journalJournal articleResearchpeer-review

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. Copyright (c) 2007 John Wiley & Sons, Ltd.
Original languageEnglish
JournalJournal of Molecular Recognition
Volume20
Issue number6
Pages (from-to)554-560
ISSN0952-3499
DOIs
Publication statusPublished - 2007
Externally publishedYes

Keywords

  • Biochemistry
  • Genetics
  • Molecular Biology
  • Structural Biology
  • Computer Vision and Pattern Recognition
  • Immunology
  • Atomic force microscopy
  • Force spectroscopy
  • Lateral membrane structure
  • Ligand-receptor interaction
  • Phospholipase A 2
  • Single molecules
  • Surfactant protein D
  • 1,2 oleoylphosphatidylcholine
  • 1,2-oleoylphosphatidylcholine
  • carbohydrate
  • cell surface receptor
  • ligand
  • phosphatidylcholine
  • surfactant protein D
  • unclassified drug
  • atomic force microscopy
  • biological model
  • carbohydrate metabolism
  • cell membrane
  • chemistry
  • conference paper
  • fluorescence microscopy
  • metabolism
  • methodology
  • physiology
  • protein binding
  • protein tertiary structure
  • ultrastructure
  • Carbohydrate Metabolism
  • Carbohydrates
  • Cell Membrane
  • Ligands
  • Microscopy, Atomic Force
  • Microscopy, Fluorescence
  • Models, Biological
  • Phosphatidylcholines
  • Protein Binding
  • Protein Structure, Tertiary
  • Pulmonary Surfactant-Associated Protein D
  • Receptors, Cell Surface
  • H026DM5V6U 1,2-oleoylphosphatidylcholine
  • ATOMIC-FORCE MICROSCOPE
  • PHOSPHOLIPASE A(2)
  • DYNAMIC STRENGTH
  • LIPID FILMS
  • SPECTROSCOPY
  • BONDS
  • CHOLESTEROL
  • CALIBRATION
  • KINETICS
  • ADHESION
  • force spectroscopy
  • ligand-receptor interaction
  • lateral membrane structure
  • phospholipase A(2)
  • single molecules
  • ligand receptor interaction
  • membrane structure
  • ligand receptor
  • protein D
  • 10060, Biochemistry studies - General
  • 10068, Biochemistry studies - Carbohydrates
  • atomic force microscopy laboratory techniques, imaging and microscopy techniques
  • time-resolved fluorescence microscopy laboratory techniques, imaging and microscopy techniques
  • Biochemistry and Molecular Biophysics
  • Methods and Techniques

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