title: Surface plasmon resonance imaging analysis of protein binding to a sialoside-based carbohydrate microarray.
abstract: Monitoring multiple biological interactions in a multiplexed array format has numerous advantages. However, converting well-developed surface chemistry for spectroscopic measurements to array-based, high-throughput screening is not a trivial process and often proves to be the bottleneck in method development. This chapter reports the fabrication and characterization of a new carbohydrate microarray with synthetic sialosides for surface plasmon resonance imaging analysis of lectin-carbohydrate interactions. Contact printing of functional sialosides on neutravidin-coated surfaces was carried out and the properties of the resulting elements were characterized by fluorescence microscopy. Sambucus nigra agglutinin (SNA) was used for testing on four different carbohydrate-functionalized surfaces and differential binding was analyzed. Multiplexed detection of SNA/biotinylated sialoside interactions on arrays up to 400 elements has been performed with good data correlation, demonstrating the effectiveness of the biotin-neutravidin-based biointerface to control probe orientation for reproducible and efficient protein binding to carbohydrates.
authors: Department of Chemistry, University of California, Riverside, CA, USA.
authors: Matthew J
authors: MJ
authors: Linman
authors: Hai
authors: H
authors: Yu
authors: Xi
authors: X
authors: Chen
authors: Quan
authors: Q
authors: Cheng
mesh_terms: D002241:Carbohydrates / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D046228:Microarray Analysis / Q000379:methods*; D011485:Protein Binding; D020349:Surface Plasmon Resonance
chemical_list: D002241:Carbohydrates; D037102:Lectins