Researchers at the University of Illinois Chicago have actually discovered that a natural peptide from fruit flies, named drosocin, can bind to bacterias ribosomes and prevent protein production, therefore requiring bacterial cells to self-destruct. This finding, together with the understanding of its working mechanism, could assist in the development of brand-new antibiotics.
A brand-new study reports on peptides anti-bacterial mechanism.
Researchers from the University of Illinois Chicago have discovered that a peptide stemmed from fruit flies may pave the way for the development of novel antibiotics.
Published in Nature Chemical Biology, their study exposes that the natural peptide, called drosocin, safeguards the insect against bacterial infections by binding onto bacterial ribosomes. When bound, drosocin avoids the ribosome from properly completing its main job– making new proteins, which cells require to function.
Protein production can be stopped by interfering with different stages of translation– the process by which DNA is “translated” into protein particles. When the ribosome reaches the stop signal at the end of the gene, the UIC scientists found that drosocin binds to the ribosome and hinders translation termination.
” Drosocin is only the 2nd peptide antibiotic understood to stop translation termination,” said Alexander Mankin, research study author and Distinguished Professor from the Center for Biomolecular Sciences and the department of pharmaceutical sciences in the College of Pharmacy. The other, called apidaecin and discovered in honeybees, was very first explained by UIC researchers in 2017.
The UIC laboratory, which is co-run by Mankin and Nora Vázquez-Laslop, research study professor in the College of Pharmacy, handled to produce the fruit fly peptide and numerous its mutants straight in bacterial cells.
” Drosocin and its active mutants made inside the bacteria forced bacterial cells to self-destruct,” Mankin said.
While the drosocin and apidaecin peptides work the very same method, the researchers found that their chemical structures and the methods they bind to the ribosome are various.
” By understanding how these peptides work, we wish to utilize the exact same mechanism for potential brand-new prescription antibiotics. Comparing side-by-side the elements of the two peptides helps with engineering new prescription antibiotics that take the very best from each,” Mankin stated.
Reference: “Inhibition of translation termination by the antimicrobial peptide Drosocin” by Kyle Mangano, Dorota Klepacki, Irueosa Ohanmu, Chetana Baliga, Weiping Huang, Alexandra Brakel, Andor Krizsan, Yury S. Polikanov, Ralf Hoffmann, Nora Vázquez-Laslop and Alexander S. Mankin, 30 March 2023, Nature Chemical Biology.DOI: 10.1038/ s41589-023-01300-x.
The study was funded by the National Institutes of Health.
