Binding kinetics of bisintercalator Triostin a with optical tweezers force mechanics.

Biophysical Journal
Christoph KleimannDario Anselmetti

Abstract

The binding kinetics of the intercalative binding of Triostin A to lambda-DNA was investigated by measuring the force extension response of the DNA-ligand complexes with an optical tweezers system. These force response curves, containing the information about different binding properties, were analyzed based on a recent method (put forth by another research group) for monointercalators that was extended to bisintercalators. Our binding analysis reveals an exponential dependence of the association constant on the applied external force as well as a decreasing binding site size. In general, our results are in agreement with those for the monointercalator ethidium. However, to explain the high-force binding site size, a new model for bisintercalation of Triostin A at high forces is proposed.

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Citations

May 14, 2014·Marine Drugs·Javier FernándezFelipe Lombó
Jun 7, 2011·Journal of Biomedical Optics·Ashis Gopal BanerjeeSatyandra K Gupta
Jun 26, 2010·Physics of Life Reviews·Kathy R ChaurasiyaMark C Williams
May 31, 2015·European Biophysics Journal : EBJ·Shreyasi ThakurMarcelo Nöllmann
Apr 18, 2016·Nucleic Acids Research·Ali A AlmaqwashiMark C Williams
Oct 21, 2016·Biophysical Journal·Ying WangDario Anselmetti
Mar 31, 2016·Biophysical Journal·Ali A AlmaqwashiMark C Williams
Mar 3, 2017·European Biophysics Journal : EBJ·Ying WangDario Anselmetti
Aug 11, 2011·Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry·Chandrashekhar U MuradeMartin L Bennink
Jul 19, 2019·Biochemistry·Yinan WangBenjamin T Goult

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