  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.
