Gupta V K, Skaife J J, Dubrovsky T B, Abbott N L
Department of Chemical Engineering and Materials Science, University of California, Davis, CA 95616, USA.
Science. 1998 Mar 27;279(5359):2077-80. doi: 10.1126/science.279.5359.2077.
Liquid crystals (LCs) were used to amplify and transduce receptor-mediated binding of proteins at surfaces into optical outputs. Spontaneously organized surfaces were designed so that protein molecules, upon binding to ligands hosted on these surfaces, triggered changes in the orientations of 1- to 20-micrometer-thick films of supported LCs, thus corresponding to a reorientation of approximately 10(5) to 10(6) mesogens per protein. Binding-induced changes in the intensity of light transmitted through the LC were easily seen with the naked eye and could be further amplified by using surfaces designed so that protein-ligand recognition causes twisted nematic LCs to untwist. This approach to the detection of ligand-receptor binding does not require labeling of the analyte, does not require the use of electroanalytical apparatus, provides a spatial resolution of micrometers, and is sufficiently simple that it may find use in biochemical assays and imaging of spatially resolved chemical libraries.
液晶(LCs)被用于将表面受体介导的蛋白质结合放大并转化为光学输出。设计了自发组织的表面,使得蛋白质分子在与这些表面上的配体结合时,触发1至20微米厚的支撑液晶薄膜取向的变化,因此每个蛋白质对应约10⁵至10⁶个液晶元的重新取向。通过液晶传输的光强度的结合诱导变化肉眼很容易看到,并且可以通过设计表面进一步放大,使得蛋白质 - 配体识别导致扭曲向列型液晶解开扭曲。这种检测配体 - 受体结合的方法不需要对分析物进行标记,不需要使用电分析仪器,提供微米级的空间分辨率,并且足够简单,可能会用于生化分析和空间分辨化学文库的成像。