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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Monoclonal Antibody Aggregation Associated with Free Radical Induced Oxidation.

Kai Zheng1, Diya Ren2, Y John Wang1

  • 1Pharmaceutical Development, Genentech, South San Francisco, CA 94080, USA.

International Journal of Molecular Sciences
|April 30, 2021
PubMed
Summary

Oxidative stress can cause therapeutic protein aggregation through methionine, tryptophan, and tyrosine modifications. Certain excipients like tryptophan can effectively reduce this protein aggregation, improving drug stability.

Keywords:
excipientfree radicalmonoclonal antibodyoxidationprotein aggregation

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Pharmaceutical Sciences

Background:

  • Protein oxidation is a critical degradation pathway for therapeutic proteins.
  • Oxidation can negatively impact drug efficacy and patient safety.
  • Understanding oxidation mechanisms is crucial for biopharmaceutical development.

Purpose of the Study:

  • To investigate the impact of oxidative stress on therapeutic antibodies.
  • To elucidate the mechanisms of oxidative-stress induced protein aggregation.
  • To identify excipients that can mitigate protein aggregation.

Main Methods:

  • Utilized 2,2'-azobis (2-amidinopropane) dihydrochloride (AAPH) to induce oxidative stress.
  • Employed size-exclusion chromatography and multi-angle light scattering to analyze protein aggregates.
  • Applied sodium dodecyl sulfate polyacrylamide gel electrophoresis and intrinsic fluorescence spectroscopy to study aggregation mechanisms.

Main Results:

  • Observed oxidation of methionine (Met) and tryptophan (Trp) residues, alongside increased protein aggregation.
  • Identified soluble aggregates including dimers, tetramers, and higher-order species.
  • Determined that inter-molecular disulfide bonds and tyrosine (Tyr) residue dimerization contribute to aggregation.

Conclusions:

  • Oxidative stress induces protein aggregation via modifications of Met, Trp, and Tyr residues.
  • Excipients such as Trp, pyridoxine, and Tyr can effectively reduce oxidative-stress induced aggregation.
  • Findings offer strategies to minimize aggregation in therapeutic protein development and storage.