Unknown

Dataset Information

0

An efficient method for the in vitro production of azol(in)e-based cyclic peptides.


ABSTRACT: Heterocycle-containing cyclic peptides are promising scaffolds for the pharmaceutical industry but their chemical synthesis is very challenging. A new universal method has been devised to prepare these compounds by using a set of engineered marine-derived enzymes and substrates obtained from a family of ribosomally produced and post-translationally modified peptides called the cyanobactins. The substrate precursor peptide is engineered to have a non-native protease cleavage site that can be rapidly cleaved. The other enzymes used are heterocyclases that convert Cys or Cys/Ser/Thr into their corresponding azolines. A macrocycle is formed using a macrocyclase enzyme, followed by oxidation of the azolines to azoles with a specific oxidase. The work is exemplified by the production of 17 macrocycles containing 6-9 residues representing 11 out of the 20 canonical amino acids.

SUBMITTER: Houssen WE 

PROVIDER: S-EPMC4282754 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications


Heterocycle-containing cyclic peptides are promising scaffolds for the pharmaceutical industry but their chemical synthesis is very challenging. A new universal method has been devised to prepare these compounds by using a set of engineered marine-derived enzymes and substrates obtained from a family of ribosomally produced and post-translationally modified peptides called the cyanobactins. The substrate precursor peptide is engineered to have a non-native protease cleavage site that can be rapi  ...[more]

Similar Datasets

| S-EPMC5853369 | biostudies-literature
| S-EPMC6208650 | biostudies-literature
| S-EPMC1829324 | biostudies-literature
| S-EPMC8562596 | biostudies-literature
| S-EPMC3189636 | biostudies-literature
| S-EPMC3574231 | biostudies-literature
| S-EPMC9066754 | biostudies-literature
| S-EPMC6010433 | biostudies-literature
2023-06-01 | GSE202764 | GEO
| S-EPMC5693220 | biostudies-literature