Washington, Oct 2 (IANS) A new breakthrough opens the way for creation of less resistant and more effective antibiotics.
“As bacteria become more resistant… our discovery provides a starting point for a completely novel class of antibiotics,” said John H. Bushweller, professor, molecular physiology, Virginia University (UV).
What Bushweller and fellow researchers at the UV and Harvard Medical School have determined is the structure of a particular integral membrane enzyme, called DsbB – one of the many proteins that reside in cell membranes.
These so-called integral membrane proteins are important, because they account for roughly a third of any genome in the human body and are the targets of more than half of all currently used drugs, according to an UV release.
Until now, scientists have been unable to acquire much structural information about these types of proteins; yet determining a protein’s structure is vital in order to understand how it functions and how it can potentially operate as a drug target.
Bushweller led study represents the first time scientists have cracked the code required to solve a certain class of membrane protein structure by using nuclear magnetic resonance (NMR) spectroscopy, the pre-eminent technique for determining the structure of organic compounds.
“What this means is that not only did we establish NMR spectroscopy as a potent tool for the characterisation of the structure, dynamics and function of integral membrane proteins, but we also discovered that the DsbB enzyme is an exciting… agent for the creation of novel antibiotics,” said Bushweller. “This could give us the roadmap to an entirely new class of antibiotics.”
These findings appeared in a recent issue of Molecular Cell.