Detection and localization of single molecular recognition events using atomic force microscopy.
Because of its piconewton force sensitivity and nanometer positional accuracy, the atomic force microscope (AFM) has emerged as a powerful tool for exploring the forces and the dynamics of the interaction between individual ligands and receptors, either on isolated molecules or on cellular surfaces. These studies require attaching specific biomolecules or cells on AFM tips and on solid supports and measuring the unbinding forces between the modified surfaces using AFM force spectroscopy. In this review, we describe the current methodology for molecular recognition studies using the AFM, with an emphasis on strategies available for preparing AFM tips and samples, and on procedures for detecting and localizing single molecular recognition events.
Hinterdorfer
Peter
P
Institute for Biophysics, Johannes Kepler University of Linz, Altenbergerstr. 69, A-4040 Linz, Austria. peter.hinterdorfer@jku.at
Dufrêne
Yves F
YF
D000818:Animals; D001665:Binding Sites; D019921:Biotinylation; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008024:Ligands; D018625:Microscopy, Atomic Force / Q000295:instrumentation / Q000379:methods*; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods*; D009844:Oligosaccharides / Q000378:metabolism; D010449:Peptide Mapping; D010455:Peptides / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism* / Q000648:ultrastructure
D008024:Ligands; D009844:Oligosaccharides; D010455:Peptides; D011956:Receptors, Cell Surface