A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance.

  title={A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance.},
  author={G. Sigal and C. Bamdad and A. Barberis and J. Strominger and G. Whitesides},
  journal={Analytical chemistry},
  volume={68 3},
This paper reports the generation of a self-assembled monolayer (SAM) that selectively binds proteins whose primary sequence terminates with a His-tag: a stretch of six histidines commonly incorporated in recombinant proteins to simplify purification. The SAM was prepared by the adsorption onto a gold surface of a mixture of two alkanethiols: one thiol that terminated with a nitrilotriacetic acid (NTA) group, a group that forms a tetravalent chelate with Ni(II), and a second thiol that… Expand
Development of a metal-chelated plasmonic interface for the linking of His-peptides with a droplet-based surface plasmon resonance read-off scheme.
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Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins.
The electrochemical stability and response towards a redox mediator of the COO-Ni(ii)-terminated SAM indicated that this platform could be easily coupled to an electrochemical method to detect bio-recognition events. Expand
Controlled immobilization of His-tagged proteins for protein-ligand interaction experiments using Ni²⁺-NTA layer on glass surfaces.
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