Department of Biochemistry, University of Illinois, Urbana, Illinois 61801, USA.
J Am Chem Soc. 2009 Dec 30;131(51):18202-3. doi: 10.1021/ja907066r.
Inhibitors and activators of protein-protein interactions are valuable as biological probes and medicinal agents but are often difficult to identify. Herein we describe a high-throughput assay, based upon photonic crystal (PC) biosensors, for the identification of modulators of protein-protein interactions. Through the use of a d-biotin-tris-NTA (BTN) hybrid compound, any His6-tagged protein can be immobilized on the surface of a PC biosensor. Binding of the bound protein to its cognate partner is detected via a shift in the peak wavelength value. We demonstrate this assay with three protein-protein pairs (caspase-9-XIAP, caspase-7-XIAP, FKBP12-FRB) and their small molecule modulators.
蛋白质-蛋白质相互作用的抑制剂和激活剂可用作生物探针和药物，但通常难以识别。在此，我们描述了一种基于光子晶体（PC）生物传感器的高通量测定法，用于鉴定蛋白质-蛋白质相互作用的调节剂。通过使用 d-生物素三-NTA（BTN）杂合物，可以将任何 His6 标签蛋白固定在 PC 生物传感器的表面上。通过检测峰波长值的变化来检测结合蛋白与其同源伴侣的结合。我们用三个蛋白质-蛋白质对（caspase-9-XIAP、caspase-7-XIAP、FKBP12-FRB）及其小分子调节剂对该测定法进行了验证。
