Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface

The Journal of Physical Chemistry. B
Mahreen AroojRicardo L Mancera

Abstract

The adsorption of proteins at the interface between two immiscible electrolyte solutions has been found to be key to their bioelectroactivity at such interfaces. Combined with interfacial complexation of organic phase anions by cationic proteins, this adsorption process may be exploited to achieve nanomolar protein detection. In this study, replica exchange molecular dynamics simulations have been performed to elucidate for the first time the molecular mechanism of adsorption and subsequent unfolding of hen egg white lysozyme at low pH at a polarized 1,2-dichloroethane/water interface. The unfolding of lysozyme was observed to occur as soon as it reaches the organic-aqueous interface, which resulted in a number of distinct orientations at the interface. In all cases, lysozyme interacted with the organic phase through regions rich in nonpolar amino acids, such that the side chains are directed toward the organic phase, whereas charged and polar residues were oriented toward the aqueous phase. By contrast, as expected, lysozyme in neat water at low pH does not exhibit significant structural changes. These findings demonstrate the key influence of the organic phase upon adsorption of lysozyme under the influence of an electric fie...Continue Reading

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Citations

Mar 16, 2017·Physical Chemistry Chemical Physics : PCCP·Giovanni B BrandaniDavid L Cheung
Nov 23, 2017·The Journal of Chemical Physics·David L Cheung
Jan 23, 2021·Langmuir : the ACS Journal of Surfaces and Colloids·Rajat Dandekar, Arezoo M Ardekani

Related Concepts

Ethylene dichloride, ion (1+)
Adsorption
Ethylene Dichlorides
Hydrogen-Ion Concentration
Leftose
Surface Properties
Molecular Dynamics
Protein Unfolding
Adsorption
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