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Clinical antibody constant regions show significant stability differences across allotypes. This study reveals IgG3 subclasses are least stable, impacting antibody developability and function.

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Area of Science:

  • Biochemistry
  • Immunology
  • Protein Engineering

Background:

  • Clinical monoclonal antibodies utilize constant regions derived from limited IgG allotypes.
  • Existing knowledge acknowledges potential impacts of allotypic diversity on antibody function and developability.
  • Data on the stability of variants with these allotypic mutations is scarce.

Purpose of the Study:

  • To systematically compare the stability of various IgG constant region allotypes.
  • To investigate the impact of allotypic variation on antibody structural dynamics and unfolding propensity.
  • To evaluate the utility of Red Edge Excitation Shift (REES) for antibody stability profiling.

Main Methods:

  • Generation of a panel of IgG1, IgG2, and IgG3 antibodies encompassing 32 unique constant region alleles.
  • Application of Red Edge Excitation Shift (REES) to measure antibody structural dynamics via tryptophan fluorescence.
  • Analysis of REES data to assess antibody flexibility and unfolding propensity.

Main Results:

  • Significant stability differences were observed across IgG subclasses, with IgG3 exhibiting the lowest overall stability.
  • High-resolution profiling revealed distinct stability profiles for individual allotypes within each subclass.
  • Observed stability variations were independent of N297-linked glycan heterogeneity.

Conclusions:

  • Naturally occurring constant domain allotypes exhibit diverse stability and dynamics.
  • REES is a valuable technique for rapid and sensitive antibody stability assessment using standard spectrophotometry.
  • Understanding allotype-specific stability is crucial for optimizing antibody developability and function.