FRET Reveals the Formation and Exchange Dynamics of Protein-Containing Complex Coacervate Core Micelles.
Langmuir
; 34(40): 12083-12092, 2018 10 09.
Article
en En
| MEDLINE
| ID: mdl-30212214
ABSTRACT
The encapsulation of proteins into complex coacervate core micelles (C3Ms) is of potential interest for a wide range of applications. To address the stability and dynamic properties of these polyelectrolyte complexes, combinations of cyan, yellow, and blue fluorescent proteins were encapsulated with cationic-neutral diblock copolymer poly(2-methyl-vinyl-pyridinium)128- b-poly(ethylene-oxide)477. Förster resonance energy transfer (FRET) allowed us to determine the kinetics of C3M formation and of protein exchange between C3Ms. Both processes follow first-order kinetics with relaxation times of ±100 s at low ionic strength ( I = 2.5 mM). Stability studies revealed that 50% of FRET was lost at I = 20 mM, pointing to the disintegration of the C3Ms. On the basis of experimental and theoretical considerations, we propose that C3Ms relax to their final state by association and dissociation of near-neutral soluble protein-polymer complexes. To obtain protein-containing C3Ms suitable for applications, it is necessary to improve the rigidity and salt stability of these complexes.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Polietilenglicoles
/
Polivinilos
/
Proteínas Fluorescentes Verdes
/
Micelas
Idioma:
En
Revista:
Langmuir
Asunto de la revista:
QUIMICA
Año:
2018
Tipo del documento:
Article