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Competing aggregation pathways for monoclonal antibodies.

Haixia Wu1, Rachel Kroe-Barrett2, Sanjaya Singh2

  • 1Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19711, USA; Department of Biotherapeutics, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, USA.

FEBS Letters
|February 18, 2014
PubMed
Summary
This summary is machine-generated.

Monoclonal antibody (MAb) aggregation occurs due to local unfolding in both the antigen binding fragment (Fab) and crystallizable fragment (Fc) regions. These regions are prone to aggregation and compete within the same MAb.

Keywords:
AggregationHot-spotMAb

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Pharmaceutical Sciences

Background:

  • Protein aggregation is a critical issue in the development and stability of monoclonal antibodies (MAbs).
  • Local unfolding of antibody regions, specifically the crystallizable fragment (Fc) and antigen binding fragment (Fab), has been historically implicated in MAb aggregation.
  • Previous studies have yielded conflicting results regarding the specific contributions of Fc and Fab regions to MAb aggregation.

Purpose of the Study:

  • To quantitatively assess and compare the aggregation kinetics of isolated Fc, isolated Fab, and intact MAb.
  • To investigate the influence of pH on the aggregation propensity of different MAb components.
  • To elucidate the competitive roles of Fc and Fab regions in the overall MAb aggregation process.

Main Methods:

  • Utilized accelerated stability studies involving high-temperature conditions.
  • Separately quantified aggregation kinetics for isolated Fc, isolated Fab, and intact MAb.
  • Varied pH conditions to assess their impact on aggregation rates.

Main Results:

  • Both isolated Fc and isolated Fab regions demonstrate significant aggregation propensity.
  • The aggregation kinetics of Fc and Fab regions were found to be pH-dependent.
  • Evidence suggests that Fc and Fab regions actively compete in the aggregation process within the intact MAb.

Conclusions:

  • Both Fc and Fab fragments are intrinsically prone to aggregation.
  • The pH significantly influences the aggregation behavior of individual MAb components.
  • Understanding the competitive aggregation of Fc and Fab is crucial for MAb stability and formulation.