AVIA Biosystems Automates Protein Stability Studies

New firm develops instrument for reliable chemical denaturation methods

The new Model 2304 Automated Protein Denaturation System completely automates protein stability determinations using chemical denaturation, and is both the first instrument of its kind and the first instrument to be introduced by AVIA Biosystems of Norton, Mass.   Developed to facilitate the formulation of biologics in a safe and stable form, the system uses intrinsic or extrinsic fluorescence to monitor the conformational changes associated with protein unfolding (denaturation) and automatically generates complete protein stability curves.

Up to 96 different formulations, process conditions or individual protein constructs can be evaluated for relative stability, and an individual stability curve generated for each.  Sample preparation, data collection, data analysis and stability report-generation are all automated.  The free energy (ΔG) of protein unfolding is automatically calculated for each formulation condition or each individual protein construct.

Chemical denaturation, a well-established technique, provides reliable thermodynamic values for protein stability and allows solution conditions such as buffer composition, buffer strength, pH, ionic strength, excipient composition, excipient concentration and protein concentration to be effectively assessed and optimized.

“Our team’s long experience in life science instrument and systems development and our established relationships with pharmaceutical industry and academic scientists enabled us develop the 2304 and to directly address this important need in the development of safe and effective biologics,” said Rick Brown, president and co-founder of AVIA Biosystems.

In pharmaceutical discovery and development settings, large numbers of constructs or formulations need to be rapidly and easily compared (rank-ordered) for stability.  For these applications, automated chemical denaturation provides the most powerful and convenient means to assess protein stability.  This technique is a perfect complement to thermal denaturation techniques and provides an independent (orthogonal) means of denaturation that can be used at meaningful temperatures (e.g. storage or physiological temperatures) eliminating the need to extrapolate from temperatures (Tm’s) that may be 30 – 50o C from the temperatures of interest.  Furthermore, in many cases chemical denaturation is completely reversible, allowing rigorous thermodynamic analysis – another important advantage.

The AVIA Biosystems Model 2304 makes, for the first time, protein chemical denaturation available in a completely automated and integrated instrument.