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Biophys. J. BioFAST: First Published July 22, 2005. doi:10.1529/biophysj.105.066795
© 2005 by the Biophysical Society.

A more recent version of this article appeared on September 1, 2005.
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Julian Gonska
Martin Stelzle
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Measuring single-bond rupture forces using high electric fields in micro-fluidic channels and DNA-oligomers as force tags

Stefanie Breisch 1, Julian Gonska 1, Helmut Deissler 2 and Martin Stelzle 1*

1 Naturwissenschaftliches und Medizinisches Institut
2 University Ulm

* To whom correspondence should be addressed. E-mail: stelzle{at}nmi.de.

Submitted on May 18, 2005
Revised on June 28, 2005
Accepted on 30 June 2005


  Abstract
The disruption force of specific biotin-streptavidin bonds was determined using DNA-oligomers as force tags. Forces were generated by an electric field acting on a biotinylated fluorescently labeled DNA-oligomer. DNA-oligomers were immobilized via biotin-streptavidin bonds on the walls of micro-fluidic channels. Channel layout and fluid-based deposition process were designed to enable well-defined localized deposition of the oligomers in a narrow gap of the micro-channel. Electric fields of up to 400V/cm were applied and electric field induced desorption of DNA-oligomers was observed. At T = 30° C field induced desorption of both a 12mer as well as a 48mer yielded a streptavidin-biotin disruption force of 75fN. Streptavidin functionalized surfaces remained intact and could be reloaded with biotinylated oligomers. At approx. 20°C, however, no field induced unbinding of the oligomers was observed at electric field strength of up to 400V/cm, indicating a significant temperature dependence of the bond strength.

Key Words: DNA oligomer, electric field, micro-channel, single-bond forces, streptavidin-biotin bond




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E. B. Walton, S. Lee, and K. J. Van Vliet
Extending Bell's Model: How Force Transducer Stiffness Alters Measured Unbinding Forces and Kinetics of Molecular Complexes
Biophys. J., April 1, 2008; 94(7): 2621 - 2630.
[Abstract] [Full Text] [PDF]


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Copyright © 2005 by the Biophysical Society.