Surface Plasmon Resonance (SPR) has been considered as a leading instrumentation for direct, label-free detection of recognition and binding events between a target analyte (antigens, hormones, DNAs, etc.) and its corresponding receptor (antibodies, capture probe DNA, proteins etc.) immobilized to the surface/liquid interface. Conventional SPR systems are based on a glass technology, in which p-polarized light, is directed through a glass prism and reflected from a gold film deposited on the prism surface. SPR effect causes a dip in angular (wavelength) dependence of the reflected light intensity with the resulting position extremely sensitive to the refractive index and the thickness of the thin biolayer. This remarkable property has been employed towards the development of SPR- based biosensors1'2, for real-time characterization of biological interactions on the gold surface (for review, see, e.g. Ref. 3).