Thursday, 2 June 2016

Development of a new antibioticsacific


Researchers have discovered a molecular structure that could aid the design of broad-spectrum antibiotics targeting an enzyme essential to every known strain of bacteria. They've mapped the structure of that enzyme, called MraY, as it is bound to the natural antibacterial muraymycin. The results show the enzyme changes it shape to reveal a hidden binding pocket, which muraymycin connects to like a two-pronged plug inserting into a socket.

By capturing the interactions between bacteria and their natural killers, researchers think they can provide the inspiration for developing new and improved drugs. For instance, five different naturally-occurring antibiotics target MraY, an enzyme responsible for building up the cell wall to shield bacteria from outside attack. However, without knowing the structures involved, researchers have been unable to develop drugs with the same effects.

For further details, see:

Ben C. Chung, Ellene H. Mashalidis, Tetsuya Tanino, Mijung Kim, Akira Matsuda, Jiyong Hong, Satoshi Ichikawa, Seok-Yong Lee. Structural insights into inhibition of lipid I production in bacterial cell wall synthesis. Nature, 2016; DOI: 10.1038/nature17636

Posted by Dr. Tim Sandle