In order to deal with the arsenal of bacteria, scientists have taken various different approaches. They no longer develop and improve traditional antibiotics but look to some of the natural antimicrobial substances through recombinant dog proteins. Some of them are fragments of proteins, known as peptide. Recently, researchers from the Massachusetts Institute of Technology, University of Brasilia and the University of British Columbia in Canada designed an antimicrobial peptide that can eliminate many bacteria, including drug-resistant bacteria. This result was published in the Nature Publishing Group Scientific Reports.
Many organisms naturally produce antimicrobial peptides, which are part of the body's own immune system, not only to destroy invading bacteria, but also kill other microorganisms, including fungi and viruses. They have the advantage of acting on bacteria through a number of different mechanisms. First, they can drill holes in the cell membrane that invades the bacteria and can destroy multiple targets, including DNA, RNA, and proteins when inside the bacteria. Second, they can activate the body's own immune system and call the white blood cells to completely eradicate the invasion of microorganisms. This is also the biggest difference between these peptides and traditional antibiotics. In addition, they can also inhibit the immune system due to excessive systemic sepsis.
Naturally-produced antimicrobial peptides are usually composed of 20 amino acids, which include a positively-charged region to help punch in the cell membrane and a hydrophobic region so that it can smoothly go through the cell membrane into the bacteria inside. With the development of modern computing technology, scientists can replace or add new amino acids to transform the natural antibacterial peptides and even design and manufacture of new antibacterial peptides so that they become more lethal.
In this study, the scientists improved based on antibacterial peptide clavanin-A found in the body of a marine organism sea squirt, including the addition of five hydrophobic amino acids to make the entire polypeptide more easily to go into the bacteria. They called the new antibacterial peptides clavanin-MO. In mice, clavanin-MO was found to abolish resistant E. coli and Staphylococcus aureus strains. It also destroys biofilms formed by bacteria on the surface of objects, such as biofilm formed by Pseudomonas aeruginosa found in the lungs of patients with cystic fibrosis.
"Our goal is to find solutions to antibiotic resistance," said Cesar de la Fuente, Ph.D., one of the authors of the paper. Drug-resistant bacteria are expected to exceed cancer and become the number one killer of human health. Antibacterial polypeptide provides an effective alternative: a molecule that can kill resistant bacteria and boost immunity and prevent excessive immune responses."
The researchers plan to further improve the design of antibacterial peptides and eventually put into clinical use. They believe that if combined with traditional antibiotics, it can be more effective in the eradication of bacteria and prevent new drug resistance. Flarebio offers good-quality recombinant proteins like recombinant CDH11.
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