A single targeted mutation is enough to alter a natural peptide system so that it also incorporates non-natural amino acids into peptides, report Swiss scientists in the journal Angewandte Chemie. The mutation increases the size of the binding cavity in one domain of the system, which changes the substrate specificity. The researchers are thus able to incorporate amino acids with a specific reactive group that can later be used to easily modify the peptide. In the search for new pharmaceuticals through the use of combinatorial chemistry and screening processes, researchers are often faced with the task of modifying and varying natural substances—sometimes by adding further molecular components, for example. Highly specific coupling with molecular markers is particularly important because it allows scientists to monitor the distribution of natural substances in cells and tissues. Coupling reactions that are almost as snapping components together can be carried out by a technique known as “click chemistry”. This method encompasses broadly applicable reactions like those between alkynes and azides, which deliver high yields. Read more at: Phys.org
The post Reprogramed nonribosomal peptide synthetase incorporates amino acids with reactive sites for ‘click’ chemistry has been published on Technology Org.
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