Rapid and Selective Chemical Editing of Ribosomally Synthesized and Post-Translationally Modified Peptides (RiPPs) via CuII -Catalyzed ß-Borylation of Dehydroamino Acids.
Angew Chem Int Ed Engl
; 60(8): 3946-3950, 2021 02 19.
Article
en En
| MEDLINE
| ID: mdl-33185967
ABSTRACT
We report the fast and selective chemical editing of ribosomally synthesized and post-translationally modified peptides (RiPPs) by ß-borylation of dehydroalanine (Dha) residues. The thiopeptide thiostrepton was modified efficiently using CuII -catalysis under mild conditions and 1D/2D NMR of the purified product showed site-selective borylation of the terminal Dha residues. Using similar conditions, the thiopeptide nosiheptide, lanthipeptide nisinâ
Z, and protein SUMO_G98Dha were also modified efficiently. Borylated thiostrepton showed an up to 84-fold increase in water solubility, and minimum inhibitory concentration (MIC) assays showed that antimicrobial activity was maintained in thiostrepton and nosiheptide. The introduced boronic-acid functionalities were shown to be valuable handles for chemical mutagenesis and in a reversible click reaction with triols for the pH-controlled labeling of RiPPs.
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Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Ribosomas
/
Ácidos Borónicos
/
Cobre
/
Alanina
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2021
Tipo del documento:
Article
País de afiliación:
Países Bajos