Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions

Marie Sofie Møller; Darrell W Cockburn; Casper Wilkens

doi:10.1007/978-1-0716-3151-5_10

Surface Plasmon Resonance Analysis for Quantifying Protein-Carbohydrate Interactions

Methods Mol Biol. 2023:2657:141-150. doi: 10.1007/978-1-0716-3151-5_10.

Authors

Marie Sofie Møller¹, Darrell W Cockburn², Casper Wilkens³

Affiliations

¹ Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.
² Department of Food Science, The Pennsylvania State University, University Park, PA, USA.
³ Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark. cwil@dtu.dk.

PMID: 37149528
DOI: 10.1007/978-1-0716-3151-5_10

Abstract

During the past two decades, surface plasmon resonance (SPR) analysis has emerged as an important tool for studying protein-carbohydrate interactions, with several commercial instruments available. Binding affinities in the nM to mM range can be determined; however, there are pitfalls that require careful experimental design to avoid. Here we give an overview of each step in the SPR analysis from immobilization to data analysis, providing key points of consideration that will allow practitioners to achieve reliable and reproducible results.

Keywords: Biosensor; Carbohydrate-active enzyme; Carbohydrate-binding module; Enzyme; Protein-carbohydrate interactions; Surface plasmon resonance.

MeSH terms

Biosensing Techniques* / methods
Carbohydrates
Surface Plasmon Resonance* / methods

Substances

Carbohydrates