Detection of biomolecular binding by Fourier-Transform SPR
Surface plasmon resonance (SPR) is a widely usedlabel-free detection technique that has many applications in drugdiscovery, pharmacokinetics, systems biology and food science.The SPR technique measures the dynamics of a biomolecularinteraction at a surface, yielding kinetic association anddissociation constants. Present SPR systems measure the stepresponse of the interaction in time domain hence are subject totime-varying noise disturbances and drifts that limit theminimum-detectable mass changes. This paper presents a newsynchronous SPR technique that measures the biomolecularinteraction not in time domain, but in frequency domain with ahigh degree of rejection to uncorrelated spurious signals. The new technique was implemented using a PDMS microfluidicchemical signal modulator chip connected to a set of on-chipfunctionalized Au SPR sensing sites. Preliminary experimentalspectral data for a model system of carbonic anhydrase bindingdemonstrates the feasibility of the new spectral technique.
Layne D.Williams Renny E.Fernandez Farouk Azizi Tridib Ghosh Carlos H.Mastrangelo
University of Utah Department of Electrical and Computer Engineering Salt Lake City, UT, USA
国际会议
成都
英文
1-4
2010-06-18（万方平台首次上网日期，不代表论文的发表时间）