Intrinsically disordered protein as carbon nanotube dispersant: How dynamic interactions lead to excellent colloidal stability.
J Colloid Interface Sci
; 556: 172-179, 2019 Nov 15.
Article
en En
| MEDLINE
| ID: mdl-31445446
ABSTRACT
The rich pool of protein conformations combined with the dimensions and properties of carbon nanotubes create new possibilities in functional materials and nanomedicine. Here, the intrinsically disordered protein α-synuclein is explored as a dispersant of single-walled carbon nanotubes (SWNTs) in water. We use a range of spectroscopic methods to quantify the amount of dispersed SWNT and to elucidate the binding mode of α-synuclein to SWNT. The dispersion ability of α-synuclein is good even with mild sonication and the obtained dispersion is very stable over time. The whole polypeptide chain is involved in the interaction accompanied by a fraction of the chain changing into a helical structure upon binding. Similar to other dispersants, we observe that only a small fraction (15-20%) of α-synuclein is adsorbed on the SWNT surface with an average residence time below 10â¯ms.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Nanotubos de Carbono
/
Alfa-Sinucleína
/
Proteínas Intrínsecamente Desordenadas
Límite:
Humans
Idioma:
En
Revista:
J Colloid Interface Sci
Año:
2019
Tipo del documento:
Article