Kikkawa Yoshihiro, Tokuhisa Hideo, Shingai Hajime, Hiraishi Tomohiro, Houjou Hirohiko, Kanesato Masatoshi, Imanaka Tadayuki, Tanaka Takeshi
Nanoarchitectonics Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan.
Biomacromolecules. 2008 Aug;9(8):2126-31. doi: 10.1021/bm800162x. Epub 2008 Jul 26.
Interaction force of chitin-binding domains (ChBD1 and ChBD2) from a thermostable chitinase onto chitin surface was directly measured by atomic force microscopy (AFM) in a buffer solution. In the force curve measurement, multiple pull-off events were observed for the AFM tips functionalized with either ChBD1 or ChBD2, whereas the AFM tips terminated with nitrilotriacetic acid groups without ChBD showed no interaction peak, suggesting that the detected forces are derived from the binding functions of ChBDs onto the chitin surface. The force curve analyses indicate that the binding force of ChBD2 is stronger than that of ChBD1. This result suggests that ChBD1 and ChBD2 play different roles in adsorption onto chitin surface.
在缓冲溶液中，通过原子力显微镜（AFM）直接测量了一种耐热几丁质酶的几丁质结合结构域（ChBD1和ChBD2）与几丁质表面之间的相互作用力。在力曲线测量中，用ChBD1或ChBD2功能化的AFM针尖观察到多次脱离事件，而未连接ChBD的用次氮基三乙酸基团封端的AFM针尖未显示相互作用峰，这表明检测到的力源自ChBD与几丁质表面的结合功能。力曲线分析表明，ChBD2的结合力强于ChBD1。该结果表明，ChBD1和ChBD2在几丁质表面吸附中发挥不同作用。
