Butelase-Mediated Macrocyclization of d-Amino-Acid-Containing Peptides.
Angew Chem Int Ed Engl
; 55(41): 12802-6, 2016 10 04.
Article
en En
| MEDLINE
| ID: mdl-27624217
ABSTRACT
Macrocyclic compounds have received increasing attention in recent years. With their large surface area, they hold promise for inhibiting protein-protein interactions, a chemical space that was thought to be undruggable. Although many chemical methods have been developed for peptide macrocyclization, enzymatic methods have emerged as a promising new economical approach. Thus far, most enzymes have been shown to act on l-peptides; their ability to cyclize d-amino-acid-containing peptides has rarely been documented. Herein we show that macrocycles consisting of d-amino acids, except for the Asn residue at the ligating site, were efficiently synthesized by butelaseâ
1, an Asn/Asp-specific ligase. Furthermore, by using a peptide-library approach, we show that butelaseâ
1 tolerates most of the d-amino acid residues at the P1'' and P2'' positions.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Compuestos Macrocíclicos
/
Aminoácidos
/
Antibacterianos
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2016
Tipo del documento:
Article
País de afiliación:
Singapur