Protein unfolding and aggregation near an hydrophobic interface [TFG]

Abstract

The behaviour of proteins in a crowded environment is a relevant matter of study for biological and medical purposes. Previous results show that, when the protein concentration increases, the proteins unfold and, at higher concentration, aggregate. Here we study if the presence of a hydrophobic surface affects this sequence of events. To this goal, we simulate a coarse-grained model of a particular sequence of amino acids, with a known native structure, near an ideal hydrophobic surface in aqueous environment. We discuss how the protein folding and the aggregation depends on the temperature and the protein concentration. We find that the sequence of events of unfolding and aggregation is not affected by the hydrophobic interface for this specfic sequence of amino acids. This work opens the way for further systematic studies on this topic, with possible relevant implications in biotechnology.