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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein
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Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins.

Laura E Valenti1, Vitor L Martins, Elisa Herrera

  • 1Instituto de Investigaciones en Físico Química de Córdoba (INFIQC) CONICET-UNC, Departamento de Fisicoquímica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA Córdoba, Argentina. giacomel@fcq.unc.edu.ar.

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|April 9, 2020
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Summary

Researchers developed a versatile electrochemical bio-recognition platform using carboxylate-functionalized substrates for histidine-tagged protein detection. This His-tag-Ni(ii) interaction enables sensitive bio-affinity binding, advancing biosensor technology.

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Area of Science:

  • Surface chemistry
  • Electrochemistry
  • Biomaterials

Background:

  • Developing robust bio-recognition platforms is crucial for sensitive biosensing.
  • Existing methods often require complex surface modifications or lack versatility.

Purpose of the Study:

  • To create a simple and versatile surface modification for electrochemical bio-recognition.
  • To utilize histidine-tagged protein affinity for Ni(ii) surface sites.
  • To characterize the developed platform for biosensing applications.

Main Methods:

  • Fabrication of carboxylate-functionalized substrates via self-assembled monolayers (SAMs).
  • Characterization using Surface-Enhanced Raman Spectroscopy (SERS), Quartz Crystal Microbalance with Dissipation monitoring (QCM-D), and X-ray Absorption Near-Edge Spectroscopy (XANES).
  • Evaluation of electrochemical stability and response.

Main Results:

  • Successful formation of carboxylate-terminated SAMs and physically adsorbed films.
  • XANES confirmed the formation of a non-distorted octahedral COO-Ni(ii) complex.
  • The modified substrate demonstrated electrochemical stability and response to a redox mediator.

Conclusions:

  • The developed COO-Ni(ii) surface modification is a versatile and effective strategy for creating electrochemical bio-recognition platforms.
  • The platform facilitates His-tag protein binding via bio-affinity interactions.
  • This approach offers potential for coupling with electrochemical methods for bio-recognition event detection.