Surface plasmon resonance imaging analysis of protein binding to a sialoside-based carbohydrate microarray

Matthew J. Linman, Hai Yu, Xi Chen, Quan Cheng

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Scopus citations


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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
Number of pages12
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
ISSN (Print)10643745


  • Biointerface
  • Biosensor
  • Biotinylated sialosides
  • Carbohydrate microarray
  • Surface plasmon resonance imaging

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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