Researchers have deciphered the atomic structure of an important antibacterial peptide in the human immune system and discovered that it forms fibers with a unique structure. According to the researchers, the findings may lead to the creation of similar artificial particles that could be used for targeted treatment of infections and even cancer cells. The discovery was published this week in a leading scientific journal.
A peptide is a short chain of amino acids. Unlike proteins, which usually contain hundreds of amino acids, peptides contain at most several dozen. One of the most important groups of peptides is the antimicrobial peptides group, which is the focus of the current study. This group plays a significant role in the innate immune system and helps it cope with various bacterial infections.
The researchers focused on an active derivative of an antimicrobial peptide found in the human body that helps fight different bacteria. In research conducted at academic laboratories and particle accelerators in Europe, they discovered that one of the mechanisms this peptide uses to kill bacteria is a unique protein fiber characterized by high stability and resistance to extreme heat. The researchers mapped the self assembly structure of the fiber, a long ribbon like structure that exhibits exceptional stability under hostile conditions and adheres to bacterial cells, allowing it to attack bacteria at close range.
Following the deciphering of the fiber’s unique structure, the researchers propose a new concept for designing stable and durable artificial antibacterial peptides that could in some cases replace antibiotic treatment. This comes against the background of the fact that antibiotic treatment, although it has saved the lives of hundreds of millions over the past century, has led to the development of bacterial resistance that reduces its effectiveness. Many deaths in hospitals today are caused by infections with antibiotic resistant bacteria, resistance that developed as a result of exposure to high doses of broad spectrum antibiotics.
Peptides are currently considered a major therapeutic promise because in at least some cases they are capable of neutralizing harmful bacterial populations without causing the development of bacterial resistance to treatment. Many research groups around the world are engaged in developing peptides for medical purposes, and the engineering challenges are numerous, including efficiency, selectivity, compatibility with body tissues, bioavailability, storage stability, and stability in the body after ingestion.
According to the researchers, is an important step toward achieving these goals. The atomic and molecular structure of the natural peptides will make it possible to produce similar structures that can serve as a framework or packaging for various applications in biomedical engineering, regenerative medicine, biotechnology, and more.
The deciphering of the complex structure of the protein fiber was based on research conducted at particle accelerators in Germany and France, as well as at multiple research centers, including a structural biology center, an interdisciplinary center for life sciences and engineering, and advanced electron microscopy facilities.
Recently, a scientific microscopy association announced that it would research prize to one of the study’s authors in recognition of the research breakthrough described in the article. The committee noted that the discovery is an impressive achievement in the study of the structure of a human antimicrobial peptide and is expected to lead to a wide range of applications in biotechnology, nanotechnology, antibacterial drug development, tissue regeneration, and more.