Many important medicines, such as antibiotics and anticancer drugs, are derived from natural products from Bacteria.
Mar 22 2024Max-Planck-Gesellschaft The enzyme complexes that produce these active ingredients have a modular design that makes them ideal tools for synthetic biology. By exploring protein evolution, a team led by Helge Bode from the Max Planck Institute for Terrestrial Microbiology in Marburg, Germany, has found new "fusion sites" that enable faster and more targeted drug development.
Industry often follows the assembly line principle: components are systematically assembled into complex products, with different production lines yielding different products. However, not humans are the actual inventors of this principle, but bacteria. Non-ribosomal peptide synthetases are bacterial enzymes that, like production lines, produce an immense variety of natural products. They enable bacteria to survive in a wide variety of natural habitats.
Multitude of enzyme variants generates diversity of natural substances The research group of Helge Bode at the Max Planck Institute for Terrestrial Microbiology in Marburg is investigating the use of these enzyme systems for the targeted production of drugs in the laboratory. The researchers modify parts of the enzymes and thus the functional properties of the entire enzyme complexes in order to produce products with new properties.
Recombination following the natural model To find out which subunits of the enzyme work particularly well together, the team focused on the question: What are the positions that evolution itself applies to establish or change the new "assembly lines" to create the required active compounds? Together with the group of Georg Hochberg from the Max Planck Institute for Terrestrial Microbiology and Michael Groll Evolution-inspired engineering of nonribosomal peptide synthetases. Science.
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