UCB collaboration to support drug design

UCB collaborates with CLF and University of Strathclyde scientists to investigate proteins in support of drug design.

Scientists from the University of Strathclyde, UCB Pharma and the CLF used 2D-IR spectroscopy to quantify changes in the secondary structure of the multifunctional calcium-binding messenger protein Calmodulin (CaM).​

Making use of the CLF’s Ultra system, the team measured subtle protein conformational changes in solution, as a function of temperature and calcium (Ca2+) concentration, using 2D-IR spectroscopy in combination with multivariate analysis. This work opens up the possibility to observe structural changes of proteins in solution in real time via a label-free method.

CLF’s Ultra system, housed within the Research Complex at Harwell, is one of the world’s most sensitive 2D-IR spectrometers and is used to investigate dynamics of complex biological systems such as the protein Calmodulin studied in this experiment.

By measuring the thermal stability and Ca2+ - binding transition of human CaM with IR absorption and 2D-IR spectroscopy, the team have proved that 2D-IR can be used to reliably quantify relative changes in secondary structure elements in proteins by measuring subtle changes in the 2D-IR spectra of the amide I IR absorption band.

Not only can ultrafast 2D-IR spectroscopy of unlabelled proteins help scientists paint a broader picture of conformational change but it can also help create a platform for spatially targeted studies.

The research was supported by academic access to CLF and the full publication is available:

View in the journal Analytical Chemistry