An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
Angew Chem Int Ed Engl
; 53(51): 14171-4, 2014 Dec 15.
Article
in En
| MEDLINE
| ID: mdl-25331823
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Oxidoreductases
/
Peptide Hydrolases
/
Peptides, Cyclic
/
Azoles
/
Phosphorus-Oxygen Lyases
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2014
Document type:
Article
Country of publication:
Germany