Abstract

Glycan biosensors based on surface plasmon resonance (SPR) spectroscopy have attracted a great deal of interest due to their potential applications in numerous biological and biomedical fields. Controlled immobilization of sugar probes on a gold substrate is believed to be critical for the performance of these SPR biosensors. In this regard, herein the authors report a direct coupling of mannose probes with bovine serum albumin (BSA) layer on the gold substrate via a squaric acid-mediated reaction under mild conditions, in which the BSA layer provides not only reactive amine groups but also a nonfouling surface property. SPR measurements show that the resultant biosensor with an appropriate amount of mannose probes exhibits high affinity to its corresponding lectin (i.e., concanavalin A) and at the same time could resist nonspecific adsorption of other lectins. The limit of detection of the current SPR biosensor is 1.9 nM. Thus, the squaric acid-mediated immobilization strategy appears to be effective and useful for the fabrication of bioanalytical devices.

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