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GENTAUR Europe

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Voortstraat 49, 1910 Kampenhout BELGIUM
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    peptides-elisa-targatt-culture-pcr-knockin-mouse-targatt-knockinA new study published in the Proceedings of the National Academy of Sciences USA, PNAS, conducted by researchers at the Ruhr University in Bochum, shows how peptides can be designed so that attack bacterial cells.

    Researchers believe that the disposal of pathogenic bacteria could be done without harming human cells.

    Moreover, this type of therapy would reduce the risk of resistance that developed most pathogens to previously applied drugs.

    Previous studies have already shown that many antimicrobial peptides interact with cell membranes of the bacteria and thus perform its microbicidal effect.

    RUB team has turned his attention to the study of a peptide called MP196, which is a group of very small positively charged peptides consisting of four to ten amino acids.

    From previous studies it is known that the MP196 can cope with a variety of bacteria including some that are multi - drug-resistant, but it is unclear exactly how this process is carried out.

    Researchers have demonstrated that prevents MP196 proteins in the cell membrane of the bacteria and thereby distort two key cellular processes: cell wall biosynthesis and cell breathing.

    Through disruption of cell wall biosynthesis, the peptide interferes with the integrity of the bacterial cell, and by interfering with the cellular respiration, distorts the production of ATP, the molecule that stores the energy used by the cell.

    Scientists are confident that the MP196 offers a starting point for developing new drugs that attack specific classes of bacteria without harming human cells, but to be confirmed in their findings need to go a long way.

    The study is part of the development of innovative antibiotics.

    To solve new drugs, federal authorities need detailed information about the procedure and the effects of drugs on both pathogens and on human cells.

    Published in News