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IgG1 thioether bond formation in vivo.

Qingchun Zhang1, Matthew R Schenauer1, John D McCarter2

  • 1Departments of Process and Product Development, Thousand Oaks, California 91320.

The Journal of Biological Chemistry
|April 30, 2013
PubMed
Summary

Therapeutic antibodies can form thioether bonds in vivo, similar to in vitro. This modification occurs in circulating antibodies and endogenous immunoglobulins, with IgG1 lambda light chains showing faster conversion rates.

Keywords:
AntibodiesDisulfideDrug DevelopmentLight ChainMass Spectrometry (MS)Post Translational Modification

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Area of Science:

  • Biochemistry
  • Immunology
  • Pharmaceutical Science

Background:

  • Antibody disulfide bonds can convert to thioether bonds during manufacturing or storage.
  • This thioether formation has been observed in vitro at the LC214-HC220 position.

Purpose of the Study:

  • To investigate the in vivo formation of thioether bonds in therapeutic antibodies.
  • To determine the prevalence and kinetics of thioether formation in endogenous antibodies.
  • To explore the influence of antibody light chain type on thioether formation rates.

Main Methods:

  • Administered an IgG1κ therapeutic antibody to human subjects and monitored thioether formation.
  • Isolated and analyzed endogenous antibodies from healthy human subjects for thioether modifications.
  • Compared thioether conversion rates between IgG1 antibodies with λ and κ light chains in vivo and in vitro.
  • Conducted mechanistic studies to elucidate the pathway of thioether formation.

Main Results:

  • Thioether bonds were confirmed to form in vivo at the LC214-HC220 position of a therapeutic antibody at approximately 0.1%/day.
  • Similar thioether modifications were detected in endogenous antibodies from healthy individuals.
  • IgG1 antibodies with λ light chains exhibited faster thioether conversion rates compared to those with κ light chains, both in vivo and in vitro.
  • Mechanistic studies indicated a preference for base-catalyzed thioether formation via light chain dehydrogenation in λ light chain antibodies.

Conclusions:

  • Thioether bond formation is a relevant in vivo post-translational modification in circulating antibodies.
  • Antibody light chain isotype significantly impacts the rate of thioether formation.
  • The findings provide insights into antibody stability and potential immunogenicity concerns.