The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors
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2008
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Abstract
The development of a biosensor based on surface plasmon resonance is described for the detection of carbohydrate-binding proteins in solution on a Biacore 2000 instrument, using immobilized glycopeptides as ligands. Their selection was based on previous screenings of solid-phase glycopeptide libraries with Ricinus communis agglutinin (RCA120) and human adhesion/growth-regulatory galectin-1 (h-Gal-1). Glycopeptides were immobilized on Au sensor chips functionalized with mixed self-assembled monolayers of different ratios of 11-mercapto-1-undecanol and 11-mercaptoundecanoic acid, and of 3-mercapto-1- propanol and 11-mercaptoundecanoic acid. The biosensors were optimized for the detection of RCA120, and a detection limit of 0.13nMwas obtained. Subsequent experiments with h-Gal-1 indicated a detection limit of at least 0.9nM for this lectin. Additionally, the effect of interfering proteins on the sensitivity of the optimized biosensor was investigated.
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Maljaars, C E P, de Souza, A C, Halkes, K M, Upton, P J, Reeman, S M, André, S, Gabius, H-J, McDonnell, M B & Kamerling, J P 2008, 'The application of neoglycopeptides in the development of sensitive surface plasmon resonance-based biosensors', Biosensors and Bioelectronics, vol. 24, no. 1, pp. 60-65.