We’re hosting a lunch and learn workshop right in your backyard! Join us for this half day event and learn how our tools are changing the game in bio-logics research.
|Wednesday, May 10th||From||To|
|Registration and morning grub||10 am||10:30 am|
|Welcome||10:30 am||10:40 am|
|Teresa Silva Barata—Ipsen||10:40 am||11:10 am|
|Bob Ford—University of Manchester||11:10 am||11:40 am|
|Dan Lund—Unchained Labs||11:40 am||12:10 pm|
|Quincy Mehta—Unchained Labs||12:10 pm||12:45 pm|
|Afternoon grub and pow-wow with Unchained Team!||12:45 pm||2 pm|
Teresa S. Barata, Ipsen Bioinnovation – Using the Unit to inform process development
Ipsen is developing a multi-domain large protein drug candidate. In this study, we used the Unit to perform pH, ionic strength and concentration screenings to determine windows of operation and rationalise process development.
Particularly at purification stages, knowledge of optimal pH and ionic strength ranges can be extremely useful to design a process that not only provides optimal yields but also ensures the protein stability throughout the different steps. The data collected so far has allowed us to improve the process by improving yield and will hopefully also contribute to an improved drug product by aiding in more rational screenings at formulation stages.
Bob Ford, University of Manchester – Use of a Cys-reactive fluorescent dye (CPM) in the characterisation of purified membrane proteins
Membrane proteins are of major significance for the pharmaceutical industry but are notoriously difficult to produce, purify and study. One limiting factor is the detergent needed for membrane protein solubilisation and purification, with different optimal detergents employed at different stages. Studies of membrane protein structure and function will also typically begin with a search for an optimally-stable ortholog and/or with mutagenesis aimed at improving the solubility and stability of the target human protein. There is therefore considerable interest in assays for membrane protein stability that allow screening of detergents and different stabilized versions of the protein. Furthermore, variability in the quality of membrane protein purification batches needs to be assessed for building confidence in subsequent biophysical studies. Finally, bioactive small molecules may induce allosteric changes in the protein upon binding and hence thermostability changes can be informative about candidate compounds.