Survivin is the smallest member of the Inhibitor of Apoptosis (IAP) family with a size of 16.5 kDa. It is present as a dimer in the cytoplasm where it is involved in the regulation of apoptosis. Survivin is also present in the cell nucleus in its monomeric form where it acts as part of the chromosomal passenger complex, which has an important role in cell division. Due to the characteristics of survivin, extensive studies have been carried out and the structure is well known, however there are still details about function and dynamics that remain to be revealed.
Our aim is to identify peptides from proteins that interact with survivin and to use different biophysical methods such as MST, SAXS, NMR and x-ray crystallography to further confirm and investigate the interactions between survivin and interacting proteins. A peptide microarray has been carried out with peptides from other proteins involved in cell cycle and apoptosis. From the result of the peptide microarray a number of interacting peptides have been chosen for further biophysical studies.