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

@article{Sigal1996ASM,
  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},
  year={1996},
  volume={68 3},
  pages={
          490-7
        }
}
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.
TLDR
The Cu(2+)-NTA modified interface showed protein loading comparable to commercially available NTA chips based on dextran chemistry and can thus be regarded as an interesting alternative. Expand
Covalent affixation of histidine-tagged proteins tethered onto Ni-nitrilotriacetic acid sensors for enhanced surface plasmon resonance detection of small molecule drugs and kinetic studies of antibody/antigen interactions.
The Ni2+-histidine (His) chelation yields a more uniform and predicable orientation of immobilized protein molecules than an amine-coupling reaction in surface plasmon resonance (SPR) analyses.Expand
High-affinity chelator thiols for switchable and oriented immobilization of histidine-tagged proteins: a generic platform for protein chip technologies.
TLDR
This new platform for switchable and oriented immobilization should assist proteome-wide wide analyses of protein-protein interactions as well as structural and single-molecule studies. Expand
Self-assembled monolayers with biospecific affinity for NAD(H)-dependent dehydrogenases: Characterization by surface plasmon resonance combined with electrochemistry 'in situ'
Gold surfaces with high biospecific affinity for pyridine-nucleotide-dependent dehydrogenases have been prepared on the basis of hydrophilic alkanethiol self-assembled monolayers bearing anExpand
Fabrication of COOH-terminated self-assembled monolayers for DNA sensors
Abstract Surface-functionalization of the self-assembled monolayer (SAM) can be achieved by introducing a functional group in a molecule at the terminal. To immobilize biomolecules such asExpand
Fabrication of self-assembled protein A monolayer and its application as an immunosensor.
TLDR
The self-assembled layer of chemically modified protein A with enhanced binding capacity can be used for immunosensor fabrication and is confirmed by surface plasmon resonance (SPR) spectroscopy. Expand
Bifunctional polyacrylamide based polymers for the specific binding of hexahistidine tagged proteins on gold surfaces.
We describe a modified bifunctional analogue of polyacrylamide that spontaneously forms self-assembled polymeric thin films on Au surfaces. The film is engineered to specifically bind histidineExpand
Stable and functional immobilization of histidine-tagged proteins via multivalent chelator headgroups on a molecular poly(ethylene glycol) brush.
We present a generic approach for immobilizing oligohistidine-tagged proteins with high stability and homogeneous functionality onto glass-type surfaces. Multivalent chelator heads (MCH) carrying twoExpand
Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins.
TLDR
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.
TLDR
A novel method for the controlled oriented immobilization of His-tagged proteins on glass surfaces functionalized with a Ni²⁺-NTA layer is presented and a clear discrimination of different protein-ligand orientations by differential height measurements is shown. Expand
...
1
2
3
4
5
...

References

SHOWING 1-4 OF 4 REFERENCES
Biosens. Bioelectron. Josse, F. Anal. Chem. Biosens. Bioelectron
  • Biosens. Bioelectron. Josse, F. Anal. Chem. Biosens. Bioelectron
  • 1993
J. Mol. Cell. Probes
  • J. Mol. Cell. Probes
  • 1992
Anal. Chem
  • Anal. Chem
  • 1988
Analytical Chemistry