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Data de publicació

2021-01-03

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cc-by (c) March Pons, David et al., 2021
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/179255

Protein Unfolding and Aggregation near a Hydrophobic Interface

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Recurs relacionat

https://doi.org/10.3390/polym13010156

Resum

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.

Matèries

Proteïnes, Superfícies hidrofòbiques, Mètode de Montecarlo

Matèries (anglès)

Proteins, Hydrophobic surfaces, Monte Carlo method

Citació

Col·leccions

Articles publicats en revistes (Física de la Matèria Condensada)

Citació

MARCH PONS, David, BIANCO, Valentino and FRANZESE, Giancarlo. Protein Unfolding and Aggregation near a Hydrophobic Interface. Polymers. 2021. Vol. 13, num. 1, pags. 156. ISSN 2073-4360. [consulted: 6 of August of 2026]. Available at: https://hdl.handle.net/2445/179255

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