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Antibody Structure01:10

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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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A pharmaceutical developability perspective on antibodies with ultra-long CDRs.

Marcel Passon1, Stefaan De Smedt1, Hristo L Svilenov2

  • 1Faculty of Pharmaceutical Sciences, Ghent University, Ottergemsesteenweg 460, 9000 Ghent, Belgium.

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Summary

Antibodies with ultralong complementarity-determining regions (ulCDRs) show promising stability for drug development. Their unique ulCDRs influence colloidal properties, impacting antibody developability and self-association.

Keywords:
Antibody(s)Biopharmaceutical characterizationDevelopabilityMonoclonal antibody(s)Physical stabilityPreformulationProtein aggregationSelf-associationpH

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Area of Science:

  • Biochemistry
  • Immunology
  • Pharmaceutical Sciences

Background:

  • Antibodies with ultralong complementarity-determining regions (ulCDRs) possess unique antigen-binding capabilities.
  • The pharmaceutical potential of ulCDRs is significant, but their stability and developability are not well understood.

Purpose of the Study:

  • To systematically analyze the physical and colloidal stability of Fab fragments containing ulCDRs.
  • To evaluate ulCDR Fabs as potential therapeutic antibody candidates.

Main Methods:

  • Utilized fluorescence- and light-scattering assays to assess thermal and colloidal stability across a pH range.
  • Conducted stress and storage studies to evaluate stability under mechanical and thermal challenges.
  • Measured relative solubility to assess colloidal properties.

Main Results:

  • ulCDR Fab fragments demonstrated good thermal stability and minimal aggregation.
  • Identified ulCDRs as key determinants of weak self-association, influencing colloidal stability.
  • ulCDR Fabs maintained high stability under mechanical stress and elevated temperatures.

Conclusions:

  • ulCDR Fabs exhibit favorable overall physical stability for therapeutic applications.
  • Weak self-interactions driven by ulCDRs are critical factors differentiating antibody properties within this class.