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Probing Thermal Stability of Proteins with Temperature Scanning Viscometer
Bowen Jiang1, Amita Jain1, Yuwei Lu1
1Department of Pharmaceutical Sciences , University of Maryland , 20 North Pine Street , Baltimore , Maryland 21201 , United States.
Molecular Pharmaceutics
|July 16, 2019
Summary
A novel temperature scanning viscometer method accurately measures protein thermal stability, crucial for therapeutic biologics. This technique offers a viable alternative to traditional methods, providing insights into protein unfolding and formulation effects.
Area of Science:
- Biochemistry
- Materials Science
- Analytical Chemistry
Background:
- Protein thermal stability is vital for therapeutic biologics.
- Existing methods like DSC, DSF, and CD have limitations.
- Accurate assessment of protein stability is critical for quality control.
Purpose of the Study:
- To introduce a novel method for probing protein thermal stability using temperature scanning viscometry.
- To demonstrate the method's applicability across various protein formulations.
- To compare the novel method with established techniques for validation.
Main Methods:
- Utilizing a temperature scanning viscometer to measure viscosity changes with temperature.
- Analyzing the first derivative of viscosity versus temperature to identify protein melting points.
- Employing orthogonal techniques (UV-vis spectroscopy, DLS) for confirmation.
Main Results:
- The viscometer method accurately determined the melting temperature of bovine serum albumin (BSA), consistent with DSC.
- The method revealed microenvironment changes and formulation effects on protein stability.
- Comparable melting temperatures were observed for other proteins like lysozyme and IgG.
Conclusions:
- Temperature scanning viscometry is a feasible and effective method for assessing protein thermal stability.
- This technique can be applied to diverse protein formulations and concentrations.
- The method provides valuable insights into protein unfolding and stability relevant to biologics development.
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