Mirror-image streptavidin with specific binding to L-biotin, the unnatural enantiomer.

ABSTRACT: The streptavidin-biotin system is known to have a very high affinity and specificity and is widely used in biochemical immunoassays and diagnostics. However, this method is affected by endogenous D-biotin in serum sample measurements (biotin interference). While several efforts using alternative high-affinity binding systems (e.g., genetically modified streptavidin and biotin derivatives) have been attempted, these efforts have all led to reduction in affinity. To solve this interference issue, the enantiomer of streptavidin was synthesized, which enabled specific binding to L-biotin. We successfully obtained a functional streptavidin molecule by peptide synthesis using D-amino acids and an in vitro folding technique. Several characterizations, including size exclusion chromatography (SEC)

SUBMITTER: Suganuma M 

PROVIDER: S-EPMC9187662 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature