Streptavidin–biotin technology: improvements and innovations in chemical and biological applications

Abstract

Streptavidin and its homologs (together referred to as streptavidin) are widely used in molecular science owing to their highly selective and stable interaction with biotin. Other factors also contribute to the popularity of the streptavidin-biotin system, including the stability of the protein and various chemical and enzymatic biotinylation methods available for use with different experimental designs. The technology has enjoyed a renaissance of a sort in recent years, as new streptavidin variants are engineered to complement native proteins and novel methods of introducing selective biotinylation are developed for in vitro and in vivo applications. There have been notable developments in the areas of catalysis, cell biology, and proteomics in addition to continued applications in the more established areas of detection, labeling and drug delivery. This review summarizes recent advances in streptavidin engineering and new applications based on the streptavidin-biotin interaction.

Peptide nucleic acid probe for protein affinity purification based on biotin–streptavidin interaction and peptide nucleic acid strand hybridization

“…The tagged proteins are separated from untagged proteins by the strong interaction between the biotin on the tag and immobilized avidin or streptavidin, allowing for proteins that are unbound or nonspecifically bound to the solid support to be washed away [3]. This strong interaction, however, becomes a problem when releasing the tagged proteins from the solid support because harsh conditions are required to dissociate the biotin from the avidin or streptavidin [4,5]. These conditions have been known to generate the release of contaminants, including subunits of streptavidin, when only one of four subunits is conjugated to the solid support [6].…”

Dual-labeled time-resolved immunofluorometric assay for the determination of IgM antibodies to rubella virus and cytomegalovirus in human serum

“…Because the recombinant antigen did not contain all the epitopes of the natural antigen, we selected biotin to bind to the antigen, which minimally affected antigen activity. Additionally, Sm 3+ was used to label streptavidin to produce a streptavidinbiotin system with increased detection sensitivity and detection range while maintaining specific immune responses [27,28].…”

Metalloenzyme design and engineering through strategic modifications of native protein scaffolds

“…Anchoring of biotin conjugated metal complexes to streptavidin has proven to be a general and effective strategy [27 and 28]. For example, an organometallic pianostool complex, RhCp* biotin Cl 2 was recently incorporated into streptavidin, enabling coupling of benzhydroxamic acid and methyl acrylate (Figure 1b) [29••].…”