RT Journal Article
T1 Protein unfolding and aggregation near a hydrophobic interface
A1 March, David
A1 Bianco, Valentino
A1 Franzese, Giancarlo
AB 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.
PB MDPI
SN 2073-4360
YR 2021
FD 2021
LK https://hdl.handle.net/20.500.14352/109936
UL https://hdl.handle.net/20.500.14352/109936
LA eng
NO Polymers 2021, 13(1), 156; https://doi.org/10.3390/polym13010156
DS Docta Complutense
RD 9 abr 2025