Structural Changes in Insulin at a Soft Electrochemical Interface
Understanding the interaction of proteins at interfaces, which occurs at or within cell membranes and lipoprotein vesicles, is central to our understanding of protein function. Therefore, new experimental approaches to understand how protein structure is influenced by protein-interface interactions...
| Main Authors: | , , , |
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| Format: | Journal Article |
| Language: | English |
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AMER CHEMICAL SOC
2021
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| Subjects: | |
| Online Access: | http://hdl.handle.net/20.500.11937/89593 |
| _version_ | 1848765254718193664 |
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| author | Lamichhane, Hum Bahadur Henares, Terence G Hackett, Mark Arrigan, Damien |
| author_facet | Lamichhane, Hum Bahadur Henares, Terence G Hackett, Mark Arrigan, Damien |
| author_sort | Lamichhane, Hum Bahadur |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Understanding the interaction of proteins at interfaces, which occurs at or within cell membranes and lipoprotein vesicles, is central to our understanding of protein function. Therefore, new experimental approaches to understand how protein structure is influenced by protein-interface interactions are important. Herein we build on our previous work exploring electrochemistry at the interface between two immiscible electrolyte solutions (ITIES) to investigate changes in protein secondary structure that are modulated by protein-interface interactions. The ITIES provides an experimental framework to drive protein adsorption at an interface, allowing subsequent spectroscopic analysis (e.g., Fourier transform infrared spectroscopy) to monitor changes in protein structure. Here, we reveal that the interaction between insulin and the interface destabilizes native insulin secondary structure, promoting formation of α helix secondary structures. These structural alterations result from protein-interface rather than protein-protein interactions at the interface. Although this is an emerging approach, our results provide a foundation highlighting the value of the ITIES as a tool to study protein structure and interactions at interfaces. Such knowledge may be useful to elucidate protein function within biological systems or to aid sensor development. |
| first_indexed | 2025-11-14T11:32:20Z |
| format | Journal Article |
| id | curtin-20.500.11937-89593 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T11:32:20Z |
| publishDate | 2021 |
| publisher | AMER CHEMICAL SOC |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-895932023-01-19T07:19:31Z Structural Changes in Insulin at a Soft Electrochemical Interface Lamichhane, Hum Bahadur Henares, Terence G Hackett, Mark Arrigan, Damien Science & Technology Physical Sciences Chemistry, Analytical Chemistry 2 IMMISCIBLE ELECTROLYTES EGG-WHITE-LYSOZYME SECONDARY STRUCTURE ADSORPTION-KINETICS CIRCULAR-DICHROISM AMYLOID FIBRILS PROTEINS BEHAVIOR FTIR SPECTROSCOPY Understanding the interaction of proteins at interfaces, which occurs at or within cell membranes and lipoprotein vesicles, is central to our understanding of protein function. Therefore, new experimental approaches to understand how protein structure is influenced by protein-interface interactions are important. Herein we build on our previous work exploring electrochemistry at the interface between two immiscible electrolyte solutions (ITIES) to investigate changes in protein secondary structure that are modulated by protein-interface interactions. The ITIES provides an experimental framework to drive protein adsorption at an interface, allowing subsequent spectroscopic analysis (e.g., Fourier transform infrared spectroscopy) to monitor changes in protein structure. Here, we reveal that the interaction between insulin and the interface destabilizes native insulin secondary structure, promoting formation of α helix secondary structures. These structural alterations result from protein-interface rather than protein-protein interactions at the interface. Although this is an emerging approach, our results provide a foundation highlighting the value of the ITIES as a tool to study protein structure and interactions at interfaces. Such knowledge may be useful to elucidate protein function within biological systems or to aid sensor development. 2021 Journal Article http://hdl.handle.net/20.500.11937/89593 10.1021/acs.analchem.1c00657 English AMER CHEMICAL SOC fulltext |
| spellingShingle | Science & Technology Physical Sciences Chemistry, Analytical Chemistry 2 IMMISCIBLE ELECTROLYTES EGG-WHITE-LYSOZYME SECONDARY STRUCTURE ADSORPTION-KINETICS CIRCULAR-DICHROISM AMYLOID FIBRILS PROTEINS BEHAVIOR FTIR SPECTROSCOPY Lamichhane, Hum Bahadur Henares, Terence G Hackett, Mark Arrigan, Damien Structural Changes in Insulin at a Soft Electrochemical Interface |
| title | Structural Changes in Insulin at a Soft Electrochemical Interface |
| title_full | Structural Changes in Insulin at a Soft Electrochemical Interface |
| title_fullStr | Structural Changes in Insulin at a Soft Electrochemical Interface |
| title_full_unstemmed | Structural Changes in Insulin at a Soft Electrochemical Interface |
| title_short | Structural Changes in Insulin at a Soft Electrochemical Interface |
| title_sort | structural changes in insulin at a soft electrochemical interface |
| topic | Science & Technology Physical Sciences Chemistry, Analytical Chemistry 2 IMMISCIBLE ELECTROLYTES EGG-WHITE-LYSOZYME SECONDARY STRUCTURE ADSORPTION-KINETICS CIRCULAR-DICHROISM AMYLOID FIBRILS PROTEINS BEHAVIOR FTIR SPECTROSCOPY |
| url | http://hdl.handle.net/20.500.11937/89593 |