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Originally published as Biophys J. BioFAST on July 22, 2005.
doi:10.1529/biophysj.105.066795
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Biophysical Journal 89:L19-L21 (2005)
© 2005 The Biophysical Society

Measuring Single-Bond Rupture Forces Using High Electric Fields in Microfluidic Channels and DNA Oligomers as Force Tags

Stefanie Breisch *, Julian Gonska *, Helmut Deissler {dagger} and Martin Stelzle *

* Naturwissenschaftliches und Medizinisches Institut, 72770 Reutlingen, Germany; and {dagger} Endokrinologisches und Onkologisches Labor der Universitätsfrauenklinik Ulm, 89075 Ulm, Germany

Correspondence: Address reprint requests and inquiries to Martin Stelzle, E-mail: stelzle{at}nmi.de, Tel.: 0049 (0)7121 51530 75.

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 microfluidic 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 microchannel. Electric fields of up to 400 V/cm were applied and electric field induced desorption of DNA oligomers was observed. At T {approx} 30°C, field-induced desorption of both a 12 mer as well as a 48 mer yielded a streptavidin-biotin disruption force of 75 fN. 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 400 V/cm, indicating a significant temperature dependence of the bond strength.




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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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