Abstract
Surface based analytical tools have gained more importance for rapid, sensitive and label-free monitoring of molecular recognition events. The surface plasmon resonance (SPR) approach has played a prominent role in real time monitoring of surface binding events. This paper first provides a brief description of the existing biosensing methods. Next, an investigation of the role of thin films of gold, silver, and aluminum for protein detection in SPR biosensors is presented. It is shown that the sensitivity, which is indicated by the shift of plasmon dip, is not linearly related to the thickness of protein but quadratic over a specific range. The approach involves plotting the reflectivity curve as a function of the angle of incidence.
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