Secondary structural changes in proteins as a result of electroadsorption at aqueous-organogel interfaces
Date
2019
Authors
Booth, S.G.
Felisilda, B.M.B.
Alvarez de Eulate, E.
Gustafsson, O.J.R.
Arooj, M.
Mancera, R.L.
Dryfe, R.A.W.
Hackett, M.J.
Arrigan, D.W.M.
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Journal article
Citation
Langmuir, 2019; 35(17):5821-5829
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Abstract
The electroadsorption of proteins at aqueous−organic interfaces offers the possibility to examine protein structural rearrangements upon interaction with lipophilic phases, without modifying the bulk protein or relying on a solid support. The aqueous−organic interface has already provided a simple means of electrochemical protein detection, often involving adsorption and ion complexation; however, little is yet known about the protein structure at these electrified interfaces. This work focuses on the interaction between proteins and an electrified aqueous−organic interface via controlled protein electroadsorption. Four proteins known to be electroactiveat such interfaces were studied: lysozyme, myoglobin, cytochrome c, and hemoglobin. Following controlled protein electroadsorption onto the interface, ex situ structural characterization of the proteins by FTIR spectroscopy was undertaken,focusing on secondary structural traits within the amide I band. The structural variations observed included unfolding to form aggregated antiparallel β-sheets, where the rearrangement was specifically dependent on the interaction with the organic phase.This was supported by MALDI ToF MS measurements, which showed the formation of protein-anion complexes for three ofthese proteins, and molecular dynamic simulations, which modeled the structure of lysozyme at an aqueous−organic interface.On the basis of these findings, the modulation of protein secondary structure by interfacial electrochemistry opens up unique prospects to selectively modify proteins.
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Link to a related website: https://www.research.manchester.ac.uk/portal/en/publications/secondary-structural-changes-in-proteins-as-a-result-of-electroadsorption-at-aqueousorganogel-interfaces(69ecbd41-9c2c-4795-8cc9-cb5018cdee22).html, Open Access via Unpaywall
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Copyright 2019 American Chemical Society