A groundbreaking technique developed at The University of Manchester, which uses crystals to map ‘invisible’ parts of molecules, is set to revolutionise drug discovery.
The technique, which involves sending beams of neutrons through crystals at freezing temperatures, just a few degrees above 'absolute zero', will for the first time allow scientists to see complete structures of protein molecules, right down to the last atom.
The problem faced by scientists using current methods is the fact that it is not possible to detect every atom in a protein’s molecular structure, and the structures therefore are incomplete – making drug design more difficult.
Professor John R. Helliwell, Professor of Structural Chemistry, who led the research, said: “This has raised the stakes in the world of drug discovery. This methodology will make research in the field more powerful, more effective and more efficient.”
The breakthrough allows the molecular structures of proteins, the chemical catalysts in the body, to be studied in complete detail. In fact, experiments at the University have shown that the number of visible atoms in a molecule doubled when using the technique, compared to techniques used today.
Protein Crystallography is an important tool used to determine the three-dimensional structures of proteins. Once a pharmaceutical company has this information, it is able to tailor drugs to target specific proteins, eg interfering with the function of such proteins in infectious agents like tuberculosis - enabling the production of more effective medicines.