Journal
ACS NANO
Volume 13, Issue 4, Pages 4246-4254Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.8b09293
Keywords
human serum transferrin; nanopore; controlled dielectric breakdown; electrophoresis; protein conformation; excluded volume
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Funding
- National Science Foundation [1707818, 1712069]
- National Institutes of Health [R03EB022759]
- National Research Foundation of Korea [NRF-2015K1A4A3047100, NRF-2015M3A7B6027973, NRF-2015M3A6B3068660]
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1712069] Funding Source: National Science Foundation
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1707818] Funding Source: National Science Foundation
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In this study, we investigated the voltage and pH responsiveness of human serum transferrin (hSTf) protein using silicon nitride (SixNy) nanopores. The Fe(III)-rich holo form of hSTf was dominant when pH > pI, while the Fe(III)-free apo form was dominant when pH < pI. The translocations of hSTf were purely in an electrophoretic sense, thus depended on its pI and the solution pH. With increasing voltage, voltage driven protein unfolding became prominent which was indicated by the trends associated with change in conductance, due to hSTf translocation, and in the excluded electrolyte volume. Additionally, analysis of the translocation events of the pure apo form of hSTf showed a clear difference in the event population compared to that of the holo form. The results obtained demonstrate the successful application of nanopore devices to distinguish between the holo and apo forms of hSTf in a mixture and to analyze its folding and unfolding phenomenon over a range of pH and applied voltages.
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