Protein Unfolding and Aggregation near a Hydrophobic Interface

TL;DR

This study uses simulations to explore how a hydrophobic surface influences protein unfolding and aggregation, revealing that surface properties and environmental factors significantly affect these processes with implications for neurodegenerative diseases.

Contribution

It introduces a coarse-grained simulation model to analyze protein behavior near hydrophobic surfaces, highlighting the impact of surface and environmental parameters.

Findings

Hydrophobic surfaces alter protein unfolding pathways.

Protein aggregation is affected by surface proximity and conditions.

Results have potential implications for understanding neurodegenerative diseases.

Abstract

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.