Use of colloidal gold surface plasmon resonance peak shift to infer affinity constants from the interactions between protein antigens and antibodies specific for single or multiple epitopes
Use of colloidal gold surface plasmon resonance peak shift to infer affinity constants from the interactions between protein antigens and antibodies specific for single or multiple epitopes
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DOI：
10.1039/a804010i
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发表时间：
1998-07-01
期刊：
影响因子：
4.2
通讯作者：
Englebienne, P
中科院分区：
文献类型：
--
作者：
Englebienne, P
当单抗与其特定配体相互作用时，包被单抗的胶体金颗粒的表面等离子体共振(SPR)波长发生红移。这种位移是由配体结合引起的粒子折射率的变化引起的。这一性质被用来实时监测溶液中相互作用的缔合和解离动力学。监测是在临床化学自动分析仪中进行的，在37℃下孵育几分钟。数据处理允许计算相互作用的亲和常数。SPR波长移动不一定需要发生颗粒的凝集或聚集，因为可以在该过程中使用涂有针对配基上单个表位的一种单抗的颗粒。用这种方法测得的亲和常数与根据Scatchard图或Biacore数据计算的亲和常数相关。
The surface plasmon resonance (SPR) wavelength of colloidal gold particles coated with a monoclonal antibody is red-shifted when the antibody interacts with its specific Ligand. This shift results fr;om the change in the refractive index of the particles as induced by ligand binding. This property is used to monitor in real-time the association and dissociation kinetics of the interaction in solution. The monitoring is perfomed in a clinical chemistry automated analyzer during a few minutes of incubation at 37 degrees C. Data treatment allows calculation of the affinity constant of the interaction. The SPR wavelength shift does not necessarily require agglutination or aggregation of the particles to occur since particles coated with one monoclonal antibody specific for a single epitope on the ligand can be used in the procedure. The affinity constants measured by this procedure correlate with those calculated from Scatchard plots or BIAcore data.