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Biophys J, January 1999, p. 500-508, Vol. 76, No. 1

Reflection Interference Contrast Microscopy Combined with Scanning Force Microscopy Verifies the Nature of Protein-Ligand Interaction Force Measurements

J. K. Stuart and V. Hlady

Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112 USA

The integration of a stand-alone scanning force microscope (SFM) scanner with a reflection interference contrast microscope (RICM) makes it possible to measure directly the separation distance between the SFM probe and the sample surface. The SFM-RICM combination, when applied to the force measurements between ligand-derivatized SFM probe and a protein receptor-derivatized surface, showed that the anomalous force discontinuities often observed for such interacting pairs were indeed a real behavior characteristic of a particular experimental configuration. Apart from small discrepancies due to transient damping, commercially available cantilevers did behave in an ideal mechanical fashion, thus indicating that protein-ligand unbinding events were occurring at distances much larger than their maximum extended length. This external verification of separation distance requires a closer examination of the physical events occurring upon detachment of the surfaces. An alternative interpretation of such force measurements is proposed here in which the protein and/or ligand immobilization chemistry is called into question.

Biophys J, January 1999, p. 500-508, Vol. 76, No. 1
© 1999 by the Biophysical Society   0006-3495/99/01/500/09  $2.00


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