A Brief Introduction to the Streptavidin-Biotin System and its Usage in Modern Surface Based Assays

Abstract

This review presents the molecular basis of the high affinity between (strept)avidin and biotin as it was discovered from different protein crystal structures using wild type and mutant streptavidin. Optimization strategies for further improving the applicability of the (strept)avidin-biotin system and prospects for modulating the affinity are discussed. The characterization and the application of the streptavidin-biotin system in surface-based biosensing assays are demonstrated with selected examples focussing on surface plasmon resonance (SPR) and atomic force microscopy (AFM). Recent trends to further enhance the utility of convential SPR e.g. parallel detection of biological molecules and sensitivity enhancement towards small molecules are covered as well.