This work encompasses a comparative analysis of the properties of two optical biosensor platforms: (1) the propagating surface plasmon resonance (SPR) sensor based on a planar, thin film gold surface and (2) the localized surface plasmon resonance (LSPR) sensor based on surface confined Ag nanoparticles fabricated by nanosphere lithography. The binding of Concanavalin A (ConA) to mannose-functionalized self-assembled monolayers (SAMs) is chosen to illustrate the similarities and the differences of these sensors. A comprehensive set of non-specific binding studies demonstrate that the single transduction mechanism is due to the specific binding of ConA to the mannose-functionalized surface. Finally, an elementary (2x1) multiplexed version of a LSPR carbohydrate sensing chip to probe the simultaneous binding of ConA to mannose and galactose-functionalized SAMs is also demonstrated.
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