Protein stability is a critical factor in protein drug formulation, drug efficacy, and storage shelf life.When proteins become unstable, molecules unfold and aggregate, causing the viscosity of the protein to increase.
Aggregated proteins can cause an immune response that leads to serious side effects. This makes viscosity a key ingredient in determining protein stability, an integral part of protein formulation.
Protein stability depends on temperature, pH, concentration and many other factors. For example, as the temperature increases, protein unfolds and loses tertiary and secondary structures. As unfolding progresses, proteins begin to aggregate, which could lead to the precipitation or formation of a gel-like structure.
DETECT UNFOLDING AND DENATURATION OF PROTEINS WITH m-VROC™ VISCOMETER
When the protein compounds begin to unfold or denaturate, small changes in viscosity occur. The RheoSense m-VROC™ viscometer is designed to detect these small changes using only a small sample. This makes m-VROC™ a useful tool to investigate drug stability without needing to dilute the sample.
- Measurement of small sample volumes— as low as 20µl;
- Partial sample recovery;
- Sealed sample (no air interface);
- Viscosity range from 0.2-100,000cP (m Pas);
- Dynamic shear range from 0.5 to 1.4M s-1;
- Temperature range from 4-100°C;
- High throughput testing;
- Improves particle size measurements;
With an innovative method of viscosity measurement that uses a chip with a rectangular slit formed with glass and a monolithic Si pressure sensor array, m-VROC™ combines MEMS and microfluidic methods to deliver data with the highest accuracy and repeatability. In addition, m-VROC™ prevents any film formation which cone and plate rheometers are susceptible to. Film formation poses a threat to protein solutions.
For more information you can contact the professionals of Paralab through the 224 664 320 or through the email firstname.lastname@example.org