Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides
| Autor: | Benjamin S Bejder, Christian A. Olsen, Fabrizio Monda, Martin Saxtorph Bojer, Hanne Ingmer, Bengt H. Gless |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
biology
Biofilm Virulence Quorum Sensing General Chemistry Clostridium perfringens biology.organism_classification medicine.disease_cause Gram-Positive Bacteria Biochemistry Catalysis chemistry.chemical_compound Quorum sensing Colloid and Surface Chemistry chemistry Listeria monocytogenes Depsipeptides Thiolactone medicine Sulfhydryl Compounds Bacteria Function (biology) |
| Zdroj: | Gless, B H, Bejder, B S, Monda, F, Bojer, M S, Ingmer, H & Olsen, C A 2021, ' Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides ', Journal of the American Chemical Society, vol. 143, no. 28, pp. 10514–10518 . https://doi.org/10.1021/jacs.1c02614 |
| Popis: | Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in the regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci, for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has also been predicted to constitute a structural feature of AIPs from other genera. Here, we show that pentameric AIPs from Lactiplantibacillus plantarum, Clostridium perfringens, and Listeria monocytogenes that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of cross-species and potential cross-genus communication of bacteria and may help guide the discovery of peptide ligands to perturb their function. |
| Databáze: | OpenAIRE |
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