Dr Matthew Blakeley, Institut Laue-Langevin said: "This study perfectly illustrates the benefits of neutrons in drug design due to their unique sensitivity to hydrogen atoms. Until recently high-resolution neutron studies of large biological systems were restricted due to the size of crystals that needed to be grown and the length of time it took for the results to be collected. However, significant technical developments, led by pioneering work here at the ILL, have greatly extended the range of experiments that can be performed providing the pharma industry with a powerful new tool to improve the performance of their products."
Andrey Kovalevsky, Oak Ridge National Laboratory said: "X-ray crystallography has been playing a crucial role in the structure-guided drug design for over two decades. It provides us with a picture of how a drug molecule binds to its macromolecular target, which is usually achieved through non-covalent interactions between these two molecules. The majority of such weak intermolecular interactions involve hydrogen atoms that normally remain invisible in X-ray structures. If one knows where hydrogen atoms are located it gives a researcher a much better idea about the nature and strength of the interactions. By applying neutron crystallography we have effectively increased the clarity of this picture, because hydrogen atoms become visible in the neutron structures. It is fair to say that by using neutrons we are now able to see every atom in a protein/drug complex, all the way to the smallest atom in nature. We are confident that by combining the two crystallographic techniques it will be possible to significantly improve the method of structure-guided drug design, which will
|Contact: Jenny Chapman|
Georgia State University