Drosocin: A Potential New Antibiotic
Scientists at the University of Illinois at Chicago have discovered a peptide from fruit flies that could lead to the development of new antibiotics. In their research, published in Chemical Biology of Nature, they found that the natural peptide, called drosocin, protects the insect from bacterial infections by binding to the ribosomes of the bacteria. Drosocin prevents the ribosome from correctly completing its primary task – making new proteins, which cells need to function.
How Drosocin Works
Protein production can be stopped by interfering with the different stages of translation, the process by which DNA is “translated” into protein molecules. The UIC scientists discovered that drosocin binds to the ribosome and inhibits translation termination when the ribosome reaches the stop signal at the end of the gene. Drosocin is only the second peptide antibiotic known to arrest translational termination, the other being apidaecin found in bees, which was first described by UIC scientists in 2017.
Producing Drosocin
The UIC laboratory, co-directed by Alexander Mankin and Nora Vázquez-Laslop, succeeded in producing the fruit fly peptide and hundreds of its mutants directly in bacterial cells. Mankin said, “Drosocin and its active mutants produced within the bacterium forced the bacterial cells to self-destruct.”
Comparing Drosocin and Apidaecin
While the drosocin and apidaecin peptides work in the same way, the researchers found that their chemical structures and the ways in which they bind to the ribosome are different. “By understanding how these peptides work, we hope to harness the same mechanism for potential new antibiotics. Comparing the components of the two peptides side by side makes it easier to engineer new antibiotics that take advantage of the best of each,” Mankin said.
Research Funding
The study, “Inhibition of Translation Termination by the Antimicrobial Peptide Drosocin,” was funded by a grant from the National Institutes of Health. Study co-authors include Kyle Mangano, Dorota Klepacki, Irueosa Ohanmu, Chetana Baliga, Weiping Huang, and Yury Polikanov from UIC, and Alexandra Brakel, Andor Krizsan, and Ralf Hoffmann from the University of Leipzig.
Drosocin: Unlocking the Potential of Peptide Antibiotics
The discovery of drosocin’s potential as an antibiotic provides a glimpse into the vast potential of peptides. Peptides are short chains of amino acids, the building blocks of proteins, that are involved in various biological functions. Because of their versatility, peptides have been a focus of drug development for various diseases. However, the use of peptides for fighting bacterial infections has been limited due to the difficulties in their production and effectiveness against a broad range of bacteria.
The discovery of drosocin and its successful production in bacterial cells could pave the way for a new generation of peptide antibiotics. By understanding how drosocin works, researchers can identify similar peptides and engineer them to be more effective against different strains of bacteria.
The Potential Benefits of Peptide Antibiotics
Peptide antibiotics have several potential benefits, including being:
Effective against antibiotic-resistant bacteria: Peptides can target different parts of the bacteria compared to traditional antibiotics, making them less susceptible to resistance.
Less toxic: Peptide antibiotics are less toxic to human cells than traditional antibiotics because they are more selective in their targets.
More cost-effective: Peptide production can be cheap and scalable, making them more affordable for patients.
Final Thoughts
The discovery of drosocin’s potential as a new antibiotic is a promising development in the fight against bacterial infections. By unlocking the potential of peptide antibiotics, researchers are paving the way for a new generation of drugs that are more effective, less toxic, and more affordable. As the world faces the rise of antibiotic-resistant bacteria, the development of new antibiotics is crucial, and the potential benefits of peptide antibiotics are immense.
Summary
Scientists at the University of Illinois at Chicago have discovered that a peptide from fruit flies called drosocin could lead to the development of new antibiotics. Drosocin protects the insect from bacterial infections by binding to the ribosomes of the bacteria and preventing protein production. Researchers found that drosocin only the second peptide antibiotic known to arrest translational termination. The UIC laboratory succeeded in producing the fruit fly peptide and hundreds of its mutants directly in bacterial cells. The chemical structures and binding mechanisms of drosocin and apidaecin, the first peptide antibiotic found in bees, were found to be different, which could lead to the development of more effective antibiotics. Peptide antibiotics have several potential benefits, including being more effective against antibiotic-resistant bacteria, less toxic to human cells, and more cost-effective.
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Scientists at the University of Illinois at Chicago have discovered that a peptide from fruit flies could lead to new antibiotics.
Their research, which is published in chemical biology of nature, shows that the natural peptide, called drosocin, protects the insect from bacterial infections by binding to the ribosomes of the bacteria. Once bound, drosocin prevents the ribosome from correctly completing its primary task: making new proteins, which cells need to function.
Protein production can be stopped by interfering with the different stages of translation, the process by which DNA is “translated” into protein molecules. The UIC scientists discovered that drosocin binds to the ribosome and inhibits translation termination when the ribosome reaches the stop signal at the end of the gene.
“Drosocin is only the second peptide antibiotic known to arrest translational termination,” said Alexander Mankin, study author and Distinguished Professor in the Center for Biomolecular Sciences and department of pharmaceutical sciences in the School of Pharmacy. The other, called apidaecin and found in bees, was first described by UIC scientists in 2017.
The UIC laboratory, co-directed by Mankin and Nora Vázquez-Laslop, a research professor at the Faculty of Pharmacy, succeeded in producing the fruit fly peptide and hundreds of its mutants directly in bacterial cells.
“Drosocin and its active mutants produced within the bacterium forced the bacterial cells to self-destruct,” Mankin said.
While the drosocin and apidaecin peptides work in the same way, the researchers found that their chemical structures and the ways in which they bind to the ribosome are different.
“By understanding how these peptides work, we hope to harness the same mechanism for potential new antibiotics. Comparing the components of the two peptides side by side makes it easier to engineer new antibiotics that take advantage of the best of each,” Mankin said. .
The study, “Inhibition of Translation Termination by the Antimicrobial Peptide Drosocin,” was funded by a grant from the National Institutes of Health. Study co-authors include Kyle Mangano, Dorota Klepacki, Irueosa Ohanmu, Chetana Baliga, Weiping Huang and Yury Polikanov from UIC, and Alexandra Brakel, Andor Krizsan and Ralf Hoffmann from the University of Leipzig.
https://www.sciencedaily.com/releases/2023/06/230606111641.htm
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