In a research report entitled “Specific inhibition of the Survivin – CRM1 interaction by peptide modified molecular tweezers” published in the journal Nature Communications, scientists from Eisen University in Duisburg and other institutions revealed how to turn off the “survival protein” in cancer cells through research. Proteins can control almost all the key physiological processes in the body cells. If they do not function normally and become more or less, it will lead to the occurrence of many diseases, including cancer. Therefore, related proteins may become new important targets for scientists to develop new drugs in the field of biomedical research.
However, a large number of proteins cannot provide suitable targets for the development of traditional active ingredients, which is why researchers are developing unusual small molecules called supramolecular ligands, because these supramolecular ligands can precisely bind to the cell surface.
In this paper, the researchers used these customized molecules to successfully target the critical surface that is crucial for the survival of cancer cells. Dr. Shirley Knauer said that the protein, Survivin, was hardly found in healthy adult organisms, but its production increased in cancer cells. The researchers used a custom ligand that covers the exact location of Survivin, which activates and transports it out of the nucleus.
Each protein has a unique three-dimensional structure with some cracks on its surface, which can form the ring structure and niche. Through the calculation and analysis of protein surface, the researchers found that an important interface is located in an orderly but dynamic cycle. Using this information and further structural analysis, researchers have designed ligands that can be applied to special difficult surfaces.
Meiners, A., Bäcker, S., Hadrović, I. et al. Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezers. Nat Commun 12, 1505 (2021). doi：10.1038/s41467-021-21753-9