Highly selective directed assembly of functional actomyosin on Au surfaces
Highly selective directed assembly of functional actomyosin on Au surfaces
复制标题
DOI：
10.1021/la047227i
复制
发表时间：
2005-04-12
期刊：
影响因子：
3.9
通讯作者：
Hong, SH
中科院分区：
文献类型：
--
作者：
Manandhar, P;Huang, L;Hong, SH
将生物马达组装到固体基底的特定位置的能力是开发基于生物马达的纳米机械系统的关键。我们开发了一种方法，利用表面分子模式将来自兔骨骼肌肌球蛋白的重酶解肌球蛋白片段直接组装到Au基底的特定位置上。在这种策略中，化学导向模式的链霉亲和素直接高度特异性组装的生物素化的重肌球蛋白的基板上，一种适用于图案化的各种生物素化的分子的策略，而BSA被用来避免非特异性吸附。使用细丝滑动的体外运动性测定来确认组装的肌动球蛋白的功能性。
The capability of assembling biomotors onto specific locations of solid substrates is a key for development of biomotor-based nanomechanical systems. We developed a method to direct the assembly of the heavy meromyosin fragment from rabbit skeletal muscle myosin onto specific locations of Au substrates utilizing surface molecular patterns. In this strategy, chemically directed patterns of streptavidin were achieved to direct highly specific assembly of biotinylated heavy meromyosin on the substrates-a strategy applicable for patterning a variety of biotinylated molecules-while BSA was utilized to avoid nonspecific adsorption. In vitro motility assays of filament sliding were used to confirm functionality of assembled actomyosin.