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Speeding up biomolecular interactions by molecular sledding

Journal Article


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Abstract


  • Numerous biological processes involve association of a protein with its binding partner, an event that is preceded by a diffusion-mediated search bringing the two partners together. Often hindered by crowding in biologically relevant environments, three-dimensional diffusion can be slow and result in long bimolecular association times. Similarly, the initial association step between two binding partners often represents a rate-limiting step in biotechnologically relevant reactions. We demonstrate the practical use of an 11-a.a. DNA-interacting peptide derived from adenovirus to reduce the dimensionality of diffusional search processes and speed up associations between biological macromolecules. We functionalize binding partners with the peptide and demonstrate that the ability of the peptide to one-dimensionally diffuse along DNA results in a 20-fold reduction in reaction time. We also show that modifying PCR primers with the peptide sled enables significant acceleration of standard PCR reactions.

Authors


  •   Turkin, Alexander (external author)
  •   Zhang, Lei (external author)
  •   Marcozzi, Alessio (external author)
  •   Mangel, Walter F. (external author)
  •   Herrmann, Andreas (external author)
  •   van Oijen, Antoine M.

Publication Date


  • 2016

Citation


  • Turkin, A., Zhang, L., Marcozzi, A., Mangel, W. F., Herrmann, A. & van Oijen, A. M. (2016). Speeding up biomolecular interactions by molecular sledding. Chemical Science, 7 (2), 916-920.

Scopus Eid


  • 2-s2.0-84961291326

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=6165&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/5112

Number Of Pages


  • 4

Start Page


  • 916

End Page


  • 920

Volume


  • 7

Issue


  • 2

Place Of Publication


  • United Kingdom

Abstract


  • Numerous biological processes involve association of a protein with its binding partner, an event that is preceded by a diffusion-mediated search bringing the two partners together. Often hindered by crowding in biologically relevant environments, three-dimensional diffusion can be slow and result in long bimolecular association times. Similarly, the initial association step between two binding partners often represents a rate-limiting step in biotechnologically relevant reactions. We demonstrate the practical use of an 11-a.a. DNA-interacting peptide derived from adenovirus to reduce the dimensionality of diffusional search processes and speed up associations between biological macromolecules. We functionalize binding partners with the peptide and demonstrate that the ability of the peptide to one-dimensionally diffuse along DNA results in a 20-fold reduction in reaction time. We also show that modifying PCR primers with the peptide sled enables significant acceleration of standard PCR reactions.

Authors


  •   Turkin, Alexander (external author)
  •   Zhang, Lei (external author)
  •   Marcozzi, Alessio (external author)
  •   Mangel, Walter F. (external author)
  •   Herrmann, Andreas (external author)
  •   van Oijen, Antoine M.

Publication Date


  • 2016

Citation


  • Turkin, A., Zhang, L., Marcozzi, A., Mangel, W. F., Herrmann, A. & van Oijen, A. M. (2016). Speeding up biomolecular interactions by molecular sledding. Chemical Science, 7 (2), 916-920.

Scopus Eid


  • 2-s2.0-84961291326

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=6165&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/5112

Number Of Pages


  • 4

Start Page


  • 916

End Page


  • 920

Volume


  • 7

Issue


  • 2

Place Of Publication


  • United Kingdom