麻豆淫院

A new study from the Autonomous University of Barcelona used computational tools to explore more than 100 proteins known as glycosaminoglycan-binding proteins (HBPs), which normally aid in processes of blood clotting and inflammation.

"The research is based on a curious observation," explains UAB Department of Biochemistry and Molecular Biology researcher Marc Torrent, coordinator of the study. "Certain proteins in our bodies that bind to heparin, a molecule regulating processes such as blood clotting and inflammation, can also recognize similar structures found on the surface of dangerous bacteria."

Based on this idea, researchers identified and synthesized fragments of these proteins containing antimicrobial potential. Their research is in the journal Molecular Systems Biology.

Among the candidates selected, five peptides synthesized in the laboratory showed potent activity against gram-negative bacteria such as Escherichia coli, Pseudomonas aeruginosa and Acinetobacter baumannii, all of them responsible for serious hospital-acquired infections.

One of the peptides, which has been named HBP-5, has shown particular promise: Not only does it effectively kill bacteria in the laboratory even at very low concentrations, but it also acts as a model of sepsis in infected mice, where the treatment succeeded in significantly reducing the bacterial load in several organs.

"These peptides stand out for their potency and specificity, with a very low toxicity in human cells, indicating that they could be safe as a basis for future treatments," explains Torrent. "This opens the door to a new family of antibiotics derived from the body's own proteins, with the advantage that they can act specifically against resistant bacteria without affecting healthy cells."