High-res structural insights into a crucial bacterial enzyme have been gained by researchers from all over the world, including those from Dublin’s Trinity College. These findings may aid chemists in developing new drugs that will inhibit the enzyme and thereby suppress disease-causing bacteria. Their work is crucial because concerns about rising rates of antibiotic resistance are still growing.
In order to” look under the bacterial bonnet” and create a molecular blueprint of the full-length enzyme that could be used to design drugs that attack any structural weaknesses, the researchers, led by Martin Caffrey, Fellow Emeritus at Trinity’s School of Medicine and School for Biochemistry and Immunology, used next-generation X-ray crystallography and single particle cryo-electron microscopy techniques.
The enzyme Lnt is of enormous potential significance as a therapeutic target because it is not present in humans; rather, it only exists in bacteria and aids in the formation of stable cell membranes through which substances are transported into and out of cells. This means that any specialized drug intended to attack it should have fewer side effects on patients.
The study was recently released in the prestigious international journal Science Advances.
A post-antibiotic era, in which minor injuries and common infections could prove fatal, is looming, according to Martin Caffrey.” A number of disease-causing bacteria have developed resistance to a plethora of first-choice drugs used to treat them, and, with antimicrobial resistance on the rise in general.”
The precision to which we have resolved this potential target paints something of a” bullseye” on that target.” New drugs are therefore desperately needed, and, while the journey from providing this kind of structural blueprint to developing one can be lengthy.