Department of Physics, Experimental Biophysics and Applied Nanoscience, Bielefeld University, Bielefeld, Germany.
Biophys J. 2009 Nov 18;97(10):2780-4. doi: 10.1016/j.bpj.2009.09.001.
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.
采用光镊系统测量 DNA-配体复合物的力-延伸响应，研究了三烯菌素 A 与 λ-DNA 的嵌入结合的结合动力学。这些力响应曲线包含了不同结合特性的信息，根据另一个研究小组提出的针对单嵌入剂的最新方法（扩展到双嵌入剂）进行了分析。我们的结合分析表明，结合常数与施加的外力呈指数关系，并且结合位点的大小减小。一般来说，我们的结果与单嵌入剂吖啶的结果一致。然而，为了解释高力结合位点的大小，提出了一种新的三烯菌素 A 在高力下的双嵌入模型。
