Sugar-coated antibiotics
Researchers at the John Innes Center and the University of East Anglia have recently explained the structure and function of an enzyme involved in attaching sugars to antibiotics.
Researchers at the John Innes Center and the University of East Anglia have recently explained the structure and function of an enzyme involved in attaching sugars to antibiotics.
Many antibiotics have different carbohydrate molecules attached to them to help antibiotics get collected by the target organism or to overcome resistance. By manipulating sugar, antibiotics can restore useful features to promote resistance.
The purpose of this paper is to find out how these sugar molecules are created, and how their structures affect their biological activity. Researchers have studied a enzyme from the less studied Streptomyces species - the enzyme that makes tylosin antibiotics. The type of enzyme they studied involves making sugar molecules attached to tylosin antibiotics. By finding out how carbohydrates are made, we can make artificial sugars with different properties.
Professor Rob Field said, 'This is part of the biochemistry industry that we cannot do chemically. We need to go back to the basic principles of how these sugars gather together in nature. We want to see what happens when we wrap sugar on an antibiotic pill and what kind of sugar will be most suitable for attachment. '
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They still have not come close to producing a product on the market but are still trying to understand how to create these types of sugar at the grassroots level. 'We are still assembling the toolkit,' said Field. By creating an enzyme model, and comparing it to a related enzyme, they can identify the key parts needed for its function, and provide a basis for biochemistry that explains its creation. How exactly does carbohydrate work?
The work was co-published with Biotica - a natural pharmaceutical product company based in Cambridge, and illustrated on the front page of ChemBioChem.
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