Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface
© 2019 American Chemical Society. Protein electrochemistry studies at a polarized interface between two immiscible electrolyte solutions (ITIES) indicate that the detection mechanism of a protein at the interface involves a combination of protein-anion complexation and interfacial adsorption pro...
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| Format: | Journal Article |
| Language: | English |
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AMER CHEMICAL SOC
2019
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| Subjects: | |
| Online Access: | http://hdl.handle.net/20.500.11937/79102 |
| _version_ | 1848764001442332672 |
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| author | Arooj, Mahreen Arrigan, Damien Mancera, Ricardo |
| author_facet | Arooj, Mahreen Arrigan, Damien Mancera, Ricardo |
| author_sort | Arooj, Mahreen |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | © 2019 American Chemical Society.
Protein electrochemistry studies at a polarized interface between two immiscible electrolyte solutions (ITIES) indicate that the detection mechanism of a protein at the interface involves a combination of protein-anion complexation and interfacial adsorption processes. A detailed characterization of the protein-facilitated mechanism of ion transfer at the ITIES will allow the development of new label-free biomolecular detection tools. Molecular dynamics simulations were performed to describe the mechanism of transfer of the hydrophobic anion tetraphenylborate (TPB-) from a 1,2-dichloroethane (organic) phase to an aqueous phase mediated by lysozyme as a model protein under the action of an external electric field. The anion migrated to the protein at the interface and formed multiple contacts. The side chains of positively charged Lys and Arg residues formed electrostatic interactions with the anion. Nonpolar residues like Trp, Met, and Val formed hydrophobic contacts with the anion as it moved along the protein surface. During this process, lysozyme adopted multiple, partially unfolded conformations at the interface, all involving various anion-protein complexes with small free-energy barriers between them. The general mechanism of protein-facilitated ion transfer at a polarized liquid-liquid interface thus likely involves the movement of a hydrophobic anion along the protein surface through a combination of electrostatic and hydrophobic interactions. |
| first_indexed | 2025-11-14T11:12:25Z |
| format | Journal Article |
| id | curtin-20.500.11937-79102 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T11:12:25Z |
| publishDate | 2019 |
| publisher | AMER CHEMICAL SOC |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-791022020-08-19T04:50:44Z Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface Arooj, Mahreen Arrigan, Damien Mancera, Ricardo Science & Technology Physical Sciences Chemistry, Physical Chemistry ELECTROCHEMICAL-BEHAVIOR FORCE-FIELD DRUG-DELIVERY ADSORPTION LYSOZYME WATER DYNAMICS AGGREGATION SIMULATION © 2019 American Chemical Society. Protein electrochemistry studies at a polarized interface between two immiscible electrolyte solutions (ITIES) indicate that the detection mechanism of a protein at the interface involves a combination of protein-anion complexation and interfacial adsorption processes. A detailed characterization of the protein-facilitated mechanism of ion transfer at the ITIES will allow the development of new label-free biomolecular detection tools. Molecular dynamics simulations were performed to describe the mechanism of transfer of the hydrophobic anion tetraphenylborate (TPB-) from a 1,2-dichloroethane (organic) phase to an aqueous phase mediated by lysozyme as a model protein under the action of an external electric field. The anion migrated to the protein at the interface and formed multiple contacts. The side chains of positively charged Lys and Arg residues formed electrostatic interactions with the anion. Nonpolar residues like Trp, Met, and Val formed hydrophobic contacts with the anion as it moved along the protein surface. During this process, lysozyme adopted multiple, partially unfolded conformations at the interface, all involving various anion-protein complexes with small free-energy barriers between them. The general mechanism of protein-facilitated ion transfer at a polarized liquid-liquid interface thus likely involves the movement of a hydrophobic anion along the protein surface through a combination of electrostatic and hydrophobic interactions. 2019 Journal Article http://hdl.handle.net/20.500.11937/79102 10.1021/acs.jpcb.9b04746 English AMER CHEMICAL SOC restricted |
| spellingShingle | Science & Technology Physical Sciences Chemistry, Physical Chemistry ELECTROCHEMICAL-BEHAVIOR FORCE-FIELD DRUG-DELIVERY ADSORPTION LYSOZYME WATER DYNAMICS AGGREGATION SIMULATION Arooj, Mahreen Arrigan, Damien Mancera, Ricardo Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title | Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title_full | Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title_fullStr | Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title_full_unstemmed | Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title_short | Characterization of Protein-Facilitated Ion-Transfer Mechanism at a Polarized Aqueous/Organic Interface |
| title_sort | characterization of protein-facilitated ion-transfer mechanism at a polarized aqueous/organic interface |
| topic | Science & Technology Physical Sciences Chemistry, Physical Chemistry ELECTROCHEMICAL-BEHAVIOR FORCE-FIELD DRUG-DELIVERY ADSORPTION LYSOZYME WATER DYNAMICS AGGREGATION SIMULATION |
| url | http://hdl.handle.net/20.500.11937/79102 |