Progress in the biosynthesis of thiopeptide antibiotics at the Shanghai Institute of Organic Chemistry A comparative study of element A found that thiopeptide antibiotics originated from a precursor peptide encoded by ribosomes, including cyclization dehydration / dehydrogenation to form thiazole / imidazole rings, dehydration to form dehydrated amino acids, and [4 + 2] cyclization reactions The post-modification step constructs the characteristic structure shared by this family of compounds (Liao, R. et al. Chem. & Biol. 2009, 16, 141). According to the commonality of this biosynthesis reflected in genetic conservatism, the researchers found that multiple microorganisms have the potential to produce new thiopeptide antibiotics through genome scanning, and verified a strain based on structural analysis Micrococcin produced by Bacillus. Since its discovery and preservation, this strain has never been found to have the ability to produce thiopeptide antibiotics. Compared with chemical synthesis, the biosynthetic pathway of thiopeptide antibiotics is quite efficient and concise. There are many examples of the formation of natural products based on ribosome-dependent precursor peptides, but such a rich post-modification process has not been reported. This is a combination biosynthesis method, that is, the precursor peptide mutation and post-modification steps The combination creates an opportunity to expand the diversity of the compound structure. In addition, the conservative types corresponding to the genetic and structural characteristics of biosynthesis also provide conditions for the discovery of new thiopeptide antibiotics in the post-genomic era. This research is of great significance for the development of new thiopeptide antibiotic drugs. News background: Thiopeptide antibiotics are a kind of polypeptide natural products derived from microorganisms, rich in elemental sulfur, and highly modified in structure. This huge "family" has so far discovered more than 80 members. Despite the differences in overall structure, all members have a cyclic peptide center composed of multiple 5-membered heterocycles and dehydrated amino acids with pyridine or piperidine as the core. Most thiopeptide antibiotics have good antibacterial activity, and some members have a strong killing effect on a variety of drug-resistant conditional pathogens. Today, with the increasing spread of bacterial resistance, the medical community The renewed attention of the ancient antibiotic family. Since the first discovery of micrococcin in 1948, the complex and unique chemical structure of thiopeptide antibiotics has attracted the attention of many synthetic chemists. At present, there have been reports of total synthesis of multiple members; however, regarding its biosynthesis The approach has always been a mystery: What method does the microorganism use to produce such a complex natural product? A more general view is that the peptide chain backbone of thiopeptide antibiotics is polymerized by non-ribosome-dependent polypeptide synthetases because This approach is more compatible with highly modified skeleton features.
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