The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
A Self-Assembled Monolayer for the Binding and Study of Histidine-Tagged Proteins by Surface Plasmon Resonance
Abstract
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 terminated with a tri(ethylene glycol) group, a group that resists protein adsorption. His-tagged proteins bound to the SAM by interaction of the histidines with the two vacant sites on Ni(II) ions chelated to the surface NTA groups. Studies with model proteins showed the binding was specific for His-tagged proteins and required the presence of Ni(II) on the surface. Immobilized His-tagged proteins were kinetically stable in buffered saline at pH 7.2 but could be desorbed by treatment with 200 mM imidazole. Surface plasmon resonance studies for two model systems showed that His-tagged proteins adsorbed on the NTA-SAM retained a greater ability to participate in binding interactions with proteins in solution than protein immobilized in a thin dextran gel layer by covalent coupling.
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Cites
Surface plasmon resonance for gas detection and biosensing
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Self-citationAn RNA polymerase II holoenzyme responsive to activators
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Contact with a component of the polymerase II holoenzyme suffices for gene activation
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Self-citationThe Handbook of Surface Imaging and Visualization
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A Survey of Structure−Property Relationships of Surfaces that Resist the Adsorption of Protein
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Cooper, M. A. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd838 · Cited by 1,015
Schuck, P. (1997) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.26.1.541 · Cited by 657
Engineering Novel Metalloproteins: Design of Metal-Binding Sites into Native Protein Scaffolds
Lu, Y., Berry, S. M., & Pfister, T. D. (2001) · Chemical Reviews · doi:10.1021/cr0000574 · Cited by 375
Schmitt, L., Ludwig, M., Gaub, H. E., & Tampé, R. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76863-9 · Cited by 171
Metadata
- Authors
- Sigal, G. B., Bamdad, C., Barberis, A., Strominger, J., & Whitesides, G. M.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-02-01
- Volume
- 68
- Issue
- 3
- Pages
- 490-497
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W1968297070
- Cited by
- 498
- References
- 11
- FWCI
- 21.92
- Type
- journal article
- Language
- en
- Open access
- closed
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