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Targeted protein functionalization using His-tags.

Gavin D Meredith1, Hayley Y Wu, Nancy L Allbritton

  • 1Department of Physiology & Biophysics, University of California - Irvine, Irvine, California 92697-4560, USA. Gavin.Meredith@invitrogen.com

Bioconjugate Chemistry
|September 16, 2004
PubMed
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Researchers developed a controllable method to chemically modify recombinant proteins using a trifunctional labeling reagent that targets His-tags. This technique enables specific, controlled, and stoichiometric protein modification for biotechnological applications.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Recombinant proteins are valuable molecular components for biotechnological applications.
  • Gene sequence data growth necessitates advanced methods for protein manipulation.
  • Integrating proteins into devices requires controllable chemical modification.

Purpose of the Study:

  • To develop a controllable method for chemical modification of recombinant proteins.
  • To enable specific, regio-specific, and stoichiometric protein labeling.
  • To create functional protein-DNA conjugates for applications like protein microarrays.

Main Methods:

  • A trifunctional labeling reagent was designed and synthesized.
  • The reagent binds to a His-tag on the target protein.

Related Experiment Videos

  • A photoreactive group creates a covalent linkage, and a variable third moiety adds functionality.
  • Reagents were used to modify murine dihydrofolate reductase (mDHFR).

    • Main Results:

    • The method demonstrated specificity for His-tagged proteins.
    • Regio-specific and stoichiometric control of modification was achieved.
    • Biotinylated and oligonucleotide-conjugated mDHFR were successfully produced.
    • A protein-DNA conjugate was used to immobilize active enzyme onto microspheres.

    Conclusions:

    • The developed method allows for versatile and controlled chemical modification of His-tagged proteins.
    • This approach introduces new functionalities without compromising enzymatic activity.
    • The protein-DNA conjugate facilitates enzyme immobilization for potential protein microarray development.