| Autor: |
Torres PB; Grupo de Bionanotecnologia y Sistemas Complejos. Infap-CONICET & Facultad Regional San Rafael, Universidad Tecnológica Nacional, Av. General Urquiza 314 C.P, M5600, San Rafael, Argentina. claudionarambuena@gmail.com., Baldor S; Facultad de Ciencias Bioquímicas y Farmacéuticas, Área Fisicoquímica, Universidad Nacional de Rosario - CONICET, Rosario 2000, Argentina., Quiroga E; Instituto de Física Aplicada (INFAP), Universidad Nacional de San Luis-CONICET, San Luis D5700BWS, Argentina., Ramirez-Pastor AJ; Instituto de Física Aplicada (INFAP), Universidad Nacional de San Luis-CONICET, San Luis D5700BWS, Argentina., Spelzini D; Facultad de Ciencias Bioquímicas y Farmacéuticas, Área Fisicoquímica, Universidad Nacional de Rosario - CONICET, Rosario 2000, Argentina., Boeris V; Facultad de Ciencias Bioquímicas y Farmacéuticas, Área Fisicoquímica, Universidad Nacional de Rosario - CONICET, Rosario 2000, Argentina., Narambuena CF; Grupo de Bionanotecnologia y Sistemas Complejos. Infap-CONICET & Facultad Regional San Rafael, Universidad Tecnológica Nacional, Av. General Urquiza 314 C.P, M5600, San Rafael, Argentina. claudionarambuena@gmail.com. |
| Abstrakt: |
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. |
