Wyatt’s static Multi-Angle Light Scattering (MALS) systems further helps cancer research by studying how S100 proteins influence the oligomerization of p53 following separation by Size Exclusion Chromatography (SEC).
The superior analytical capabilities of the technology are detailed in a new application note, titled ‘Protein-Protein Interactions of Tumor Suppressor p53 with S100 Proteins’.
At its Laboratory for Molecular Biology (LMB), the MRC Centre for Protein Engineering undertakes research in an attempt to provide understanding of the thermodynamic basis for the interactions of p53 with DNA and other proteins, as well as the effects of mutation on these interactions. The aim is to develop short peptides able to rescue p53 mutants.
The S100 family is a group of dimeric, calcium-binding proteins, which have been found to be overexpressed in several types of cancer. Part of the research at the LMB is to investigate how S100 proteins bind to p53 in its different oligomeric states, using monomeric and dimeric p53 mutants.
The p53 variants have a large fraction of intrinsically disordered structure and do not elute according to globular protein standards in SEC. In response, company’s static MALS has been chosen as the ideal detection technology to study the complex formation of S100 proteins and p53 by determining the molecular weight of the complexes independently of protein standards.
The studies of the complex formation of p53 and S100 proteins by SEC-MALS instrumentation have helped the company to understand how S100 proteins influence the oligomerization of p53. Based on these results and in vivo studies, a binding model has been established where S100 proteins can activate tetrameric p53 while inhibiting p53 activity binding to the monomer by shifting the tetramerization equilibrium.
