Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface
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 n...
| Main Authors: | , , , , |
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| Format: | Journal Article |
| Published: |
American Chemical Society
2016
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| Online Access: | http://hdl.handle.net/20.500.11937/31988 |
| _version_ | 1848753537180237824 |
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| author | Arooj, M. Gandhi, N. Kreck, C. Arrigan, Damien Mancera, R. |
| author_facet | Arooj, M. Gandhi, N. Kreck, C. Arrigan, Damien Mancera, R. |
| author_sort | Arooj, M. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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 field, which results in the unfolding of its structure. (Figure Presented). |
| first_indexed | 2025-11-14T08:26:05Z |
| format | Journal Article |
| id | curtin-20.500.11937-31988 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T08:26:05Z |
| publishDate | 2016 |
| publisher | American Chemical Society |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-319882017-09-13T15:18:09Z Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface Arooj, M. Gandhi, N. Kreck, C. Arrigan, Damien Mancera, R. 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 field, which results in the unfolding of its structure. (Figure Presented). 2016 Journal Article http://hdl.handle.net/20.500.11937/31988 10.1021/acs.jpcb.6b00536 American Chemical Society restricted |
| spellingShingle | Arooj, M. Gandhi, N. Kreck, C. Arrigan, Damien Mancera, R. Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title | Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title_full | Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title_fullStr | Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title_full_unstemmed | Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title_short | Adsorption and Unfolding of Lysozyme at a Polarized Aqueous-Organic Liquid Interface |
| title_sort | adsorption and unfolding of lysozyme at a polarized aqueous-organic liquid interface |
| url | http://hdl.handle.net/20.500.11937/31988 |