- A panel of scFv mutant proteins have been studied using multiple techniques for characterizing their aggregation properties
- Supercharging proteins by mutagenesis greatly reduces aggregate growth rates, but enhances formation of small aggregates due to reducing conformational stability.
- Aggregation behaviour for multiple proteins has been investigated in solutions with different types of multivalent ionic excipients
- Poly-phosphate ions (adenosine tri-phosphate, tri-polyphosphate) are promising excipients due to their superior effectiveness at suppressing aggregate growth, and in some instances, increasing conformational stability
- A set of rules are provided for choosing ionic excipients to increase shelf stability of biopharmaceuticals.
Robin Curtis, Senior Lecturer, University of Manchester