For example, builders know that precision and special tools are required to perform the task correctly. The same is true at the molecular level when creating antibiotics (combined and other, for example, amoxil).
New data obtained at North Carolina State University demonstrates the possibility of using the enzyme as a “wrench” in the” assembly ” of an antibiotic. By modifying this enzyme, the researchers hope to develop and synthesize stronger and more adaptable antibiotics from inexpensive natural compounds.
Creating antibiotics: Cyrromycin
Cyrromycin is a well-known antibiotic that can be obtained by natural synthesis, which takes place outside the chemical laboratory. Nature creates compounds similar to cyrromycin through the sequential action of enzymes that collect the antibiotic, as on a factory conveyor belt. Each of the enzymes performs a specific function, putting different fragments of molecules together like a puzzle. If you understand this process at the molecular level, chemists will be able to use the mechanism developed by nature for the synthesis of antibiotics and antitumor drugs with less losses and costs.
Chemist Gavin Williams drew attention to one of the enzymes involved in the assembly of cyrromycin. The enzyme is named Kirkii and is responsible for placing the molecular fragment of the antibiotic in a key location. As Williams notes: “KirCII is the core enzyme of the entire complex. Natural compounds are assembled by enzymes from pieces, small modules, or blocks, bound in a certain order. Enzymes like Kirkii work on the principle of a wrench collecting these molecular fragments. Without them, the assembly of the molecule will not be completed properly.”
Williams and his team conducted a molecular analysis of KirCII to determine why and how it binds together specific protein fragments in the composition of kirromycin. It turned out that the enzyme has an electric charge on its surface, complementary to the charge on the surface of the protein, which contributes to their binding. When KirCII finds matching charges, it puts the protein in place. The scientists were able to find a charged region of KirCII that binds to the target protein. They hope to use this to create complementary charges on the surface of other proteins so that KirCII can bind them as well.
Williams says: “At the moment, KirCII is a specific “wrench”. If we modify it to fit other proteins, we can turn it into a set of different “keys” and create completely different antibiotics. Kirromycin is not very useful at the moment, but using KirCII to collect fragments of other antibiotics, we will be able to mix, combine and create new, stronger antibiotics.”