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Related Experiment Video

Updated: Apr 19, 2026

Laboratory Scale Production and Purification of a Therapeutic Antibody
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A general approach to antibody thermostabilization.

Audrey D McConnell1, Xue Zhang, John L Macomber

  • 1a AnaptysBio, Inc. ; San Diego , CA USA.

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|December 18, 2014
PubMed
Summary

Engineered antibodies demonstrate enhanced thermostability and improved affinity through a novel framework. This antibody engineering approach broadens applications and ease of use for therapeutic proteins.

Keywords:
CDR, complementarity-determining regionCH2, heavy chain constant domain 2CH3, heavy chain constant domain 3DSC, differential scanning calorimetryHC, heavy chainLC, light chainNGF, β-nerve growth factorSHM, somatic hypermutationSPR, surface plasmon resonanceTNF, tumor necrosis factorTm, melting temperatureVH, heavy chain variable regionVL, light chain variable regionaffinity maturationmonoclonal antibodiesprotein engineeringsolubilitysomatic hypermutationthermostability

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Area of Science:

  • Biotechnology
  • Protein Engineering
  • Immunology

Background:

  • Antibody thermostability is crucial for broader applications and ease of use.
  • Existing antibodies may lack sufficient stability for certain conditions.
  • Engineering approaches are needed to improve antibody biophysical characteristics.

Purpose of the Study:

  • To develop a modified human IgG framework for enhanced antibody thermostability.
  • To investigate the efficacy of CDR-grafting, mammalian cell display, and in vitro SHM for antibody stabilization and affinity maturation.
  • To assess the broad applicability of this engineering approach across diverse antibodies.

Main Methods:

  • CDR-grafting of diverse specificities onto a stable human IgG framework.
  • Utilizing mammalian cell display for antibody engineering.
  • Employing in vitro somatic hypermutation (SHM) for affinity maturation.
  • Assessing thermostability and affinity changes post-engineering.

Main Results:

  • A modified IgG framework successfully stabilized an anti-HA33 antibody by ~10°C with a 300-fold affinity increase.
  • Specificities of 10 diverse antibodies were transferred to the stable framework via CDR-grafting.
  • Eight of the 10 transferred antibodies were stabilized, including therapeutic antibodies like adalimumab (+9.9°C), denosumab (+7°C), and cetuximab (+6.9°C).

Conclusions:

  • The developed antibody engineering strategy effectively enhances thermostability and affinity.
  • This approach demonstrates broad utility for improving biophysical properties of various antibodies.
  • The engineered framework offers potential for wider antibody applications in diverse fields.