Supramolecular Control over Split-Luciferase Complementation.
Angew Chem Int Ed Engl
; 55(31): 8899-903, 2016 07 25.
Article
en En
| MEDLINE
| ID: mdl-27356091
Supramolecular split-enzyme complementation restores enzymatic activity and allows for on-off switching. Split-luciferase fragment pairs were provided with an N-terminal FGG sequence and screened for complementation through host-guest binding to cucurbit[8]uril (Q8). Split-luciferase heterocomplex formation was induced in a Q8 concentration dependent manner, resulting in a 20-fold upregulation of luciferase activity. Supramolecular split-luciferase complementation was fully reversible, as revealed by using two types of Q8 inhibitors. Competition studies with the weak-binding FGG peptide revealed a 300-fold enhanced stability for the formation of the ternary heterocomplex compared to binding of two of the same fragments to Q8. Stochiometric binding by the potent inhibitor memantine could be used for repeated cycling of luciferase activation and deactivation in conjunction with Q8, providing a versatile module for inâ
vitro supramolecular signaling networks.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Hidrocarburos Aromáticos con Puentes
/
Inhibidores Enzimáticos
/
Imidazoles
/
Luciferasas
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2016
Tipo del documento:
Article
País de afiliación:
Países Bajos
Pais de publicación:
Alemania