Twigged streptavidin polymer as a scaffold for protein assembly

Takuya Matsumoto, Yuki Isogawa, Kosuke Minamihata, Tsutomu Tanaka, Akihiko Kondo

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Protein assemblies are an emerging tool that is finding many biological and bioengineering applications. We here propose a method for the site-specific assembly of proteins on a twigged streptavidin (SA) polymer using streptavidin as a functional scaffold. SA was genetically appended with a G tag (sortase A recognition sequence) and a Y tag (HRP recognition sequence) on its N- and C-termini, respectively, to provide G-SA-Y. G-SA-Y was polymerized using HPR-mediated tyrosine coupling, then fluorescent proteins were immobilized on the polymer by biotin-SA affinity and sortase A-mediated ligation. Fluorescence measurements showed that the proteins were immobilized in close proximity to each other. Hydrolyzing enzymes were also functionally assembled on the G-SA-Y polymer. The site-specific assembly of proteins on twigged SA polymer may find new applications in various biological and bioengineering fields.

Original languageEnglish
Pages (from-to)61-66
Number of pages6
JournalJournal of Biotechnology
Volume225
DOIs
Publication statusPublished - May 10 2016
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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