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Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry
Published on: January 26, 2024
Colloidal interactions between monoclonal antibodies in aqueous solutions
Dejan Arzenšek1, Drago Kuzman, Rudolf Podgornik
1Sandoz Biopharmaceuticals Mengeš, Lek Pharmaceuticals dd, Mengeš, Slovenia. dejan.arzensek@gmail.com
Journal of Colloid and Interface Science
|July 31, 2012
Summary
Understanding protein interactions is key for stabilizing monoclonal antibodies (mAbs). This study quantifies colloidal interactions using light scattering and zeta potential, offering insights into mAb clustering control.
Area of Science:
- Biophysics
- Colloid Science
- Protein Chemistry
Background:
- Colloidal interactions govern the behavior and stability of globular proteins, including monoclonal antibodies (mAbs).
- Protein aggregation, or cluster formation, in solution is a critical concern for therapeutic protein stability.
- Understanding these interactions is vital for controlling mAb behavior in pharmaceutical formulations.
Purpose of the Study:
- To investigate and quantify the colloidal interactions between monoclonal antibodies (mAbs) in dilute solutions.
- To establish a method for indirectly determining protein-protein interactions through measurable solution properties.
- To provide a framework for controlling mAb assembly by manipulating solution parameters.
Main Methods:
- Utilized Dynamic Light Scattering (DLS) and Static Light Scattering (SLS) for high-throughput quantification of intermolecular interactions.
- Employed Laser Doppler Electrophoresis (M3-PALS) for zeta potential measurements.
- Determined the second virial coefficient (B22) as an indicator of colloidal interactions, parameterized using DLVO theory components (surface charge/potential and Hamaker coefficient) as functions of ionic strength and pH.
Main Results:
- Demonstrated a high-throughput approach for rapid, indirect determination of protein-protein colloidal interactions.
- Successfully parameterized electrostatic and van der Waals interactions based on solution conditions (ionic strength, pH).
- Established a correlation between solution parameters and mAb interaction behavior, facilitating prediction and control.
Conclusions:
- The study provides a robust method for understanding and controlling mAb colloidal interactions in solution.
- The findings enhance the comprehension of mAb assembly processes and offer practical strategies for formulation development.
- Validated the applicability of the Derjaguin-Landau-Verwey-Overbeek (DLVO) theory for describing mAb solution assembly, offering a consistency check for the model.
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