Skip NavigationSkip to Content

Antibody recognition imaging by force microscopy

  1. Author:
    Raab, A.
    Han, W. H.
    Badt, D.
    Smith-Gill, S. J.
    Lindsay, S. M.
    Schindler, H.
    Hinterdorfer, P.
  2. Author Address

    Hinterdorfer P Univ Linz, Inst Biophys A-4040 Linz Austria Univ Linz, Inst Biophys A-4040 Linz Austria Mol Imaging Corp Phoenix, AZ USA NCI, Basic Res Lab, Div Basic Sci, Frederick Canc Res & Dev Ctr,NIH Frederick, MD 21702 USA Arizona State Univ, Dept Phys & Astron Tempe, AZ 85287 USA
    1. Year: 1999
  1. Journal: Nature Biotechnology
    1. 17
    2. 9
    3. Pages: 902-905
  2. Type of Article: Article
  1. Abstract:

    We have developed a method that combines dynamic force microscopy with the simultaneous molecular recognition of an antigen by an antibody, during imaging. A magnetically oscillated atomic force microscopy tip carrying a tethered antibody was scanned over a surface to which lysozyme was bound. By oscillating the probe at an amplitude of only a few nanometers, the antibody was kept in close proximity to the surface, allowing fast and efficient antigen recognition and gentle interaction between tip and sample. Antigenic sites were evident from reduction of the oscillation amplitude, as a result of antibody-antigen recognition during the lateral scan. Lysozyme molecules bound to the surface were recognized by the antibody on the scanning tip with a few nanometers lateral resolution. In principle, any ligand can be tethered to the tip; thus, this technique could potentially be used for nanometer-scale epitope mapping of biomolecules and localizing receptor sites during biological processes. [References: 24]

    See More

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel