A streptavidin variant with slower biotin dissociation and increased mechanostability

Nat Methods. 2010 May;7(5):391-3. doi: 10.1038/nmeth.1450. Epub 2010 Apr 11.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomechanical Phenomena
  • Biotin / metabolism*
  • Biotinylation
  • Escherichia coli Proteins / metabolism
  • Membrane Proteins / metabolism
  • Microscopy, Atomic Force
  • Molecular Sequence Data
  • Protein Binding
  • Protein Engineering
  • Streptavidin / genetics*
  • Streptavidin / metabolism*


  • Escherichia coli Proteins
  • FtsK protein, E coli
  • Membrane Proteins
  • traptavidin
  • Biotin
  • Streptavidin

Associated data

  • GENBANK/GU952124