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Quantification of Protein Interactions and Solution Transport Using High-Density GMR Sensor Arrays

Monitoring the kinetics of protein interactions on a high density sensor array is vital to drug development and proteomic analysis. Label-free kinetic assays based on surface plasmon resonance are the current gold standard, but they have poor detection limits, suffer from non-specific binding, and a...

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Detalles Bibliográficos
Autores principales: Gaster, Richard S., Xu, Liang, Han, Shu-Jen, Wilson, Robert J., Hall, Drew A., Osterfeld, Sebastian J., Yu, Heng, Wang, Shan X.
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3089684/
https://www.ncbi.nlm.nih.gov/pubmed/21478869
http://dx.doi.org/10.1038/nnano.2011.45
Descripción
Sumario:Monitoring the kinetics of protein interactions on a high density sensor array is vital to drug development and proteomic analysis. Label-free kinetic assays based on surface plasmon resonance are the current gold standard, but they have poor detection limits, suffer from non-specific binding, and are not amenable to high throughput analyses. Here we show that magnetically responsive nanosensors that have been scaled to over 100,000 sensors/cm(2) can be used to measure the binding kinetics of various proteins with high spatial and temporal resolution. We present an analytical model that describes the binding of magnetically labeled antibodies to proteins that are immobilized on the sensor surface. This model is able to quantify the kinetics of antibody-antigen binding at sensitivities as low as 20 zeptomoles of solute.