Correlation Engine 2.0
Clear Search sequence regions

  • biotin (11)
  • circular dichroism (1)
  • heat (1)
  • serum (1)
  • streptavidin (8)
  • Sizes of these terms reflect their relevance to your search.

    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), circular dichroism spectra (CD), and heat denaturation experiments collectively confirmed the higher-order enantiomer of natural streptavidin had been formed with comparable stability to the natural protein. L-biotin specific binding of this novel molecule enabled us to avoid biotin interference in affinity measurements using the Biacore system and enzyme-linked immunosorbent assay (ELISA). We propose the enantiomer of streptavidin as a potential candidate to replace the natural streptavidin-biotin system, even for in vivo use. © 2022. The Author(s).


    Masatoshi Suganuma, Takuya Kubo, Kengo Ishiki, Kota Tanaka, Kouzou Suto, Daisuke Ejima, Masahiro Toyota, Kouhei Tsumoto, Toshiyuki Sato, Youichi Nishikawa. Mirror-image streptavidin with specific binding to L-biotin, the unnatural enantiomer. Scientific reports. 2022 Jun 10;12(1):9568

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 35688934

    View Full Text