Modulation of the electrostatic potential around α-lactalbumin using oligoelectrolyte chains, pH and salt concentration.
Soft Matter
; 20(9): 2100-2112, 2024 Feb 28.
Article
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| MEDLINE
| ID: mdl-38348915
ABSTRACT
In this study, we conducted a comprehensive computational investigation of the interaction between α-lactalbumin, a small globular protein, and strong anionic oligoelectrolyte chains with a polymerization degree from 2 to 9. Both the protein and oligoelectrolyte chains are represented using coarse-grained models, and their properties were calculated by the Monte Carlo method under constant pH conditions. We were able to estimate the effects of this interaction on the electrostatic potential around the protein. At acidic pH, the protein had a net positive charge; therefore, the electrostatic potential around it was also positive. To neutralize or reverse this electrostatic potential, oligoelectrolyte chains with a minimum size of six monomers were necessary. Simultaneously, low salt concentrations were required as elevated salt levels led to a significant attenuation of the electrostatic interactions and the corresponding electrostatic potential.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Cloruro de Sodio
/
Lactalbúmina
Idioma:
En
Revista:
Soft Matter
Año:
2024
Tipo del documento:
Article
País de afiliación:
Argentina