High Throughput Chemical Stability Screening for Proteins

June 23, 2020
11 am to 12 pm EDT



Webinar Description:

The new SUPR-CM from Protein Stable is a high throughput protein stability measurement screening system which uses microplates throughout the process. Unlike the vast majority of systems currently on the market the SUPR-CM has the sensitivity to read the lowest volume of samples in the plates they are prepared in, thus simplifying the process and reducing cost. Utilising a sub µL accurate sample preparation system and an advanced, highly sensitive intrinsic protein fluorescence plate reader, the SUPR-CM makes the use of chemical denaturation methods easy and scalable, with the addition of further automation.

With thermal stability measurement being a well-established tool in the optimisation of biotherapeutics as well as their formulation, the SUPR-CM can provide truly complementary information that can help identify stability parameters not otherwise identified. Thermal based methods (along with other automated chemical stability systems) are almost never able to measure the protein unfolding at true equilibrium since aggregation and the acceleration of protein degradation at high temperatures prevent this. The SUPR-CM system allows true equilibria to be reached before measurement, even in slow to equilibrate monoclonal antibody formats. Combined with thermal data, this ensures confident conclusions about the stability of a protein are made and are not artefacts of slow unfolding.

Application of the SUPR-CM in protein engineering can identify optimal candidates with high stability, before further development work in the discovery process.

Once at the formulation stage, the SUPR-CM system can be used to measure protein stability under a wide variety of conditions, finding the buffer composition that provides the most stability. As well as buffer composition, the system allows measurement of protein stability over a wide protein concentration range from 10 µg per mL to 10’s of mg/mL. Bring together the capabilities of chemical denaturation, automated liquid handling, intrinsic fluorescence microplate spectrofluorimetry and method-based characterisation of fluorescence spectra, the SUPR-CM protein stability system facilitates formulation and protein optimization at higher-throughputs and at lower sample volumes.

Learning Objectives:

  • Introduce the SUPR-CM instrument and the Protein Stable company.
  • Understand that the SUPR-CM chemical denaturant operating procedure allows an equilibrium to be established before measurement, which eliminates the errors caused by the non-equilibrium measurement of protein stability by thermal denaturation or other short chemical methods.
  • Learn how the SUPR-CM instrument combined with modern sub µL liquid dispensing solutions opens chemical denaturation as a time and sample efficient method for protein stability.
  • That the SUPR-CM system allows for scalability from a simple benchtop instrument able to run 20 samples of formulation conditions easily, to full automation allowing hundreds of samples in a day.


Dr. Lindsay Cole, PhD
Research Director, Research
Applied Photophysics Limited and Protein Stable Limited.

Lindsay gained his PhD from the University of New England in Australia before undertaking Post-Doctoral research at the University of Michigan, USA, and the University of York UK. His particular focus was enzyme structure and function relationships.

Lindsay Cole joined Applied Photophysics in 2007 as an applications scientist working in the R&D department. During this time he has played a significant role in the development of our Chirascan CD spectrometer platform. Lindsay’s first major contribution to the Company was in the design and development of the CS/SX stopped-flow accessory. He was also deeply involved with the DMS application for the Chirascan V100 CD instrument. His most significant achievement so far has been as the project leader on the development of the Chirascan Q100.

Lindsay is a founding board member of Protein stable, a joint venture between Applied photophysics and Fluorescence innovations, to apply high-end fluorescence plate reading solution for the protein stability and biophysical characterisation of protein and biopharmaceuticals.

Dr. Alastair Davy, PhD
Applications Scientist, Research
Protein Stable Limited.

Dr Alastair Douglas Davy is an Application Scientist with Protein Stable. Alastair completed his physics Masters before undertaking an interdisciplinary PhD with the OPTIMA Centre for Doctoral training program. As part of OPTIMA, Alastair obtained a business Masters in Healthcare Innovation and Entrepreneurship while researching the photophysical/structural properties of melanins using time-resolved fluorescence spectroscopy.

Outside of his academic work, Alastair completed a 3-month work placement with a Californian nanomaterial manufacturer. Alastair has also volunteered for the outreach events Explorathon and Cell Block Science, helping to communicate the latest scientific developments outside of the academic environment. As a former member of the Analytical Science Network committee, Alastair assisted in the organisation of the Emerging Analytical Professionals conference.