Favre Mélanie, Sekatskii Serguei K, Dietler Giovanni
Laboratoire de Physique de la Matière Vivante, IPMC, BSP, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Ultramicroscopy. 2008 Sep;108(10):1135-9. doi: 10.1016/j.ultramic.2008.04.058. Epub 2008 May 14.
Using single-molecule force-clamp spectroscopy, where the distance between the AFM tip and the sample surface is fixed and a few parallel avidin-biotin complexes are kept stretched by a certain force, we were able to observe the formation of single avidin-biotin bonds. Perspectives to use such an approach to study association reactions at single-molecule level in the conditions resembling those characteristic for some processes in vivo (e.g. virus-cell membrane attachment) are briefly discussed.
使用单分子力钳光谱法,其中原子力显微镜(AFM)针尖与样品表面之间的距离是固定的,并且一些平行的抗生物素蛋白-生物素复合物在一定力的作用下保持拉伸状态,我们能够观察到单个抗生物素蛋白-生物素键的形成。本文简要讨论了在类似于体内某些过程(如病毒-细胞膜附着)的特征条件下,使用这种方法在单分子水平上研究缔合反应的前景。