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Interferon dimers: IFN-PEG-IFN.

Annabelle Herrington-Symes1, Ji-Won Choi1, Steve Brocchini2

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|August 19, 2017
PubMed
Summary
This summary is machine-generated.

Recombinant protein dimers, like interferon (IFN) homo-dimers, can enhance therapeutic avidity and circulation times. Site-specific conjugation methods impact antiviral activity, with PEG size also influencing biological function.

Keywords:
Site-specific conjugationinterferonprotein dimer

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Drug Development

Background:

  • Complex protein therapeutics can be engineered by combining simpler proteins via site-specific chemical conjugation.
  • Protein dimers, such as interferon (IFN) homo-dimers, may offer enhanced avidity for cell surface receptors and prolonged circulation times.
  • Cytokine binding to cell surface receptors often involves receptor dimerization, highlighting the importance of protein structure in biological activity.

Purpose of the Study:

  • To prepare and compare the biological activity of interferon (IFN) homo-dimers synthesized through different site-specific conjugation methods.
  • To investigate the influence of polyethylene glycol (PEG) size on the antiviral activity of IFN homo-dimers.
  • To evaluate the impact of conjugation site (disulphide vs. histidine tag) on the efficacy of IFN homo-dimers.

Main Methods:

  • Preparation of IFN homo-dimers using two distinct site-specific conjugation strategies: bis-alkylation of native disulphides and conjugation to histidine tags.
  • Synthesis of control conjugates to facilitate a thorough assessment of homo-dimer activity.
  • In vitro evaluation of antiviral and antiproliferative activities of the prepared IFN homo-dimers and control conjugates.

Main Results:

  • The His8IFN-PEG20-His8IFN homo-dimer, created via histidine-specific conjugation, showed slightly higher in vitro antiviral activity than the IFN-PEG20-IFN homo-dimer produced by disulphide re-bridging.
  • Enhanced retention of activity was observed with conjugation to an N-terminal His-tag on IFN, consistent with prior findings.
  • For homo-dimers prepared by disulphide re-bridging, IFN-PEG10-IFN exhibited greater biological activity than IFN-PEG20-IFN, suggesting PEG size impacts antiviral function.

Conclusions:

  • Site-specific conjugation to histidine tags may yield more active IFN homo-dimers compared to disulphide re-bridging.
  • The size of the polyethylene glycol (PEG) linker plays a crucial role in determining the antiviral efficacy of IFN-PEG-IFN homo-dimers.
  • Engineered protein dimers represent a promising approach for developing advanced protein therapeutics with improved pharmacokinetic and pharmacodynamic properties.