A magical peptide that can effectively cope with drug-resistant bacteria

A magical peptide that can effectively cope with drug-resistant bacteria

November 11, 2016 Source: WuXi PharmaTech

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Antibiotic abuse worldwide has received a lot of attention recently. Due to the excessive use of antibiotics, more and more bacteria have developed resistance, resulting in the emergence of "super bacteria." At the same time, the development of new antibiotics has not kept pace with the evolution of bacteria. According to estimates by the World Health Organization, by 2050, there may be 10 million people worldwide who die from resistant bacteria every year.
 
In order to update the arsenal of bacteria, some scientists have taken different measures. Instead of developing improved traditional antibiotics, they turned their attention to some natural antibacterial substances, some of which are fragments of proteins called peptides. Recently, researchers from the Massachusetts Institute of Technology, the University of Brasilia in Brazil and the University of British Columbia in Canada have collaborated on the design of an antimicrobial peptide that can eliminate many kinds of bacteria, including resistant bacteria. Nature Publishing Group's publication "Scientific Reports".
 
 
â–²Multiple mechanisms of action of antimicrobial peptides (Source: Pharmaceuticals)
 
Many organisms naturally produce antibacterial peptides, which are part of the body's own immune system. They not only destroy invading bacteria, but also kill other microorganisms, including fungi and viruses. Their strength lies in the production of bacteria for many different machines. First, they can drill holes in the cell membrane of invading bacteria, and when they enter the interior of the bacteria, they can destroy multiple targets, including DNA, RNA, and proteins. Second, they activate the body's own immune system and summon white blood cells to completely destroy invading microorganisms. This is also the biggest difference between these peptides and traditional antibiotics. In addition, they can also suppress systemic sepsis due to overreaction of the immune system.
 
Naturally occurring antimicrobial peptides are usually composed of 20 amino acids, which include a positively charged region to help perforate the cell membrane, and a hydrophobic region that allows it to smoothly pass through the cell membrane into the interior of the bacteria. With the development of modern computing technology, scientists can modify natural antibacterial peptides by replacing or adding new amino acids, and even design and manufacture new antibacterial peptides, making them more lethal.
 
In this study, scientists engineered an antibacterial peptide, clavanin-A, found in marine marine sea squirts, including the addition of five hydrophobic amino acids to make the entire peptide more accessible to bacteria. They called the new antimicrobial peptide clavanin-MO. Experiments in mice have found that clavanin-MO can destroy resistant E. coli and S. aureus strains. It can also destroy biofilms formed by bacteria on the surface of objects, such as biofilms formed by Pseudomonas aeruginosa, often found in the lungs of patients with cystic fibrosis.
 
 
â–² Corresponding author of the article, Dr. Cesar de la Fuente (Source: LinkedIn)
 
One of the co-authors of the article, Dr. Cesar de la Fuente of the Massachusetts Institute of Technology, said: "Our goal is to find a solution for antibiotic resistance. Resistant bacteria are expected to surpass cancer and become the number one killer of human health. Antimicrobial peptides Provides an effective alternative. One such molecule can both kill resistant bacteria, boost immunity, and prevent excessive immune responses."
 
The researchers plan to further improve the design of antimicrobial peptides and eventually put them into clinical use. They believe that if combined with traditional antibiotics, it can kill bacteria more effectively and prevent new drug resistance.

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