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Folding and aggregation of proteins and ion transfer at electrified liquid-liquid interfaces

The adsorption of proteins at liquid interfaces is of particular biotechnological interest in various biomedical applications. The bioelectrochemical detection of proteins is indeed possible due to their role in the transfer of ions across such interfaces. The conformation adopted by proteins at a liquid interface is an essential factor that influences the stability of the interface and their ability to capture and transfer ions. The mechanism of protein adsorption and ion transfer at electrified oil-water interfaces remains however largely unknown. Molecular dynamics simulations will be used to look at the way different representative proteins interact at water-organic liquid interfaces in the presence of an electric field, the changes to their conformation and the potential aggregation that occur during this process, as well as the ability of hydrophobic anions to interact with these proteins at different pH. Understanding these processes will be useful for the optimisation of protein detection in bioelectrochemical devices for the diagnosis and tracking of therapeutic approaches.

Adsorption of lysozyme at the water-dichloroethane interface
The adsorption of lysozyme at the water-dichloroethane interface involves strong hydrophobic interactions with the organic phase which lead to the unfolding of the protein.