Protein Unfolding and Aggregation near a Hydrophobic Interface

Polymers

Valentino Bianco¹  Giancarlo Franzese²  David March² 

[1] Chemical Physics Department, Faculty of Chemistry, Universidad Complutense de Madrid, Plaza de las Ciencias, Ciudad Universitaria, 28040 Madrid, Spain;Secció de Física Estadística i Interdisciplinària—Departament de Física de la Matèria Condensada, Facultat de Física, Universitat de Barcelona, Martí i Franquès 1, 08028 Barcelona, Spain;

关键词: protein;    aggregation;    unfolding;    hydrophobic;    coarse grain;    Monte Carlo;   

DOI  :  10.3390/polym13010156

来源: DOAJ

【 摘 要 】

The behavior of proteins near interfaces is relevant for biological and medical purposes. Previous results in bulk show that, when the protein concentration increases, the proteins unfold and, at higher concentrations, aggregate. Here, we study how the presence of a hydrophobic surface affects this course of events. To this goal, we use a coarse-grained model of proteins and study by simulations their folding and aggregation near an ideal hydrophobic surface in an aqueous environment by changing parameters such as temperature and hydrophobic strength, related, e.g., to ions concentration. We show that the hydrophobic surface, as well as the other parameters, affect both the protein unfolding and aggregation. We discuss the interpretation of these results and define future lines for further analysis, with their possible implications in neurodegenerative diseases.

【 授权许可】

Unknown