Langmuir · 2007 · 39 citations · 25 references
In this letter, we report on the direct measurement of the intercalation interactions between acridine and double-stranded DNA (dsDNA) using single molecule force spectroscopy. The interaction between acridine and dsDNA is broken by force of 36 pN at a loading rate of 5.0 nN/s. The most probable rupture force between acridine and dsDNA is dependent on the loading rate, indicating that the binding of acridine and dsDNA is a dynamic process. The combination of SMFS experimental data with the theoretical model clearly suggests the presence of two energy barriers along with an unbinding trajectory of acridine-dsDNA.
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Dynamic strength of molecular adhesion bonds
E. Evans, Ken Ritchie · Biophysical Journal · 1997 · 2.5K citations · Full text
Adhesion Forces Between Individual Ligand-Receptor Pairs
Ernst‐Ludwig Florin, Vincent T. Moy, Hermann E. Gaub · Science · 1994 · 1.9K citations