A streptavidin variant with slower biotin dissociation and increased mechanostability

Claire E. Chivers, Estelle Crozat, Calvin Chu, Vincent T. Moy, David J. Sherratt, Mark Howarth

Research output: Contribution to journalArticlepeer-review

134 Scopus citations


Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.

Original languageEnglish (US)
Pages (from-to)391-393
Number of pages3
JournalNature Methods
Issue number5
StatePublished - May 2010
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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