Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide
© 2018 American Chemical Society. Phosphorus (P) recovery from wastewater is essential for sustainable P management. A biomimetic hexapeptide (SGAGKT) has been demonstrated to bind inorganic P in P-rich environments, however the dynamics and molecular mechanisms of P-binding to the hexapeptide still...
| Main Authors: | , , , , |
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| Format: | Journal Article |
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American Chemical Society
2018
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| Online Access: | http://hdl.handle.net/20.500.11937/70758 |
| _version_ | 1848762293704196096 |
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| author | Zhai, H. Qin, L. Zhang, W. Putnis, Christine Wang, L. |
| author_facet | Zhai, H. Qin, L. Zhang, W. Putnis, Christine Wang, L. |
| author_sort | Zhai, H. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | © 2018 American Chemical Society. Phosphorus (P) recovery from wastewater is essential for sustainable P management. A biomimetic hexapeptide (SGAGKT) has been demonstrated to bind inorganic P in P-rich environments, however the dynamics and molecular mechanisms of P-binding to the hexapeptide still remain largely unknown. We used dynamic force spectroscopy (DFS) to directly distinguish the P-unbound and P-bound SGAGKT adsorbed to a mica (001) surface by measuring the single-molecule binding free energy (?Gb). Using atomic force microscopy (AFM) to determine real-time step retreat velocities of triangular etch pits formed at the nanoscale on the dissolving (010) face of brushite (CaHPO4·2H2O) in the presence of SGAGKT, we observed that SGAGKT peptides promoted in situ dissolution through an enhanced P-binding driven by hydrogen bonds in a P-loop being capable of discriminating phosphate over arsenate, concomitantly forming a thermodynamically favored SGAGKT-HPO42- complexation at pH 8.0 and relatively low ionic strength, consistent with the DFS and isothermal titration calorimetry (ITC) determinations. The findings reveal the thermodynamic and kinetic basis for binding of phosphate to SGAGKT and provide direct evidence for phosphate discrimination in phosphate/arsenate-rich environments. |
| first_indexed | 2025-11-14T10:45:16Z |
| format | Journal Article |
| id | curtin-20.500.11937-70758 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T10:45:16Z |
| publishDate | 2018 |
| publisher | American Chemical Society |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-707582018-12-13T09:34:11Z Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide Zhai, H. Qin, L. Zhang, W. Putnis, Christine Wang, L. © 2018 American Chemical Society. Phosphorus (P) recovery from wastewater is essential for sustainable P management. A biomimetic hexapeptide (SGAGKT) has been demonstrated to bind inorganic P in P-rich environments, however the dynamics and molecular mechanisms of P-binding to the hexapeptide still remain largely unknown. We used dynamic force spectroscopy (DFS) to directly distinguish the P-unbound and P-bound SGAGKT adsorbed to a mica (001) surface by measuring the single-molecule binding free energy (?Gb). Using atomic force microscopy (AFM) to determine real-time step retreat velocities of triangular etch pits formed at the nanoscale on the dissolving (010) face of brushite (CaHPO4·2H2O) in the presence of SGAGKT, we observed that SGAGKT peptides promoted in situ dissolution through an enhanced P-binding driven by hydrogen bonds in a P-loop being capable of discriminating phosphate over arsenate, concomitantly forming a thermodynamically favored SGAGKT-HPO42- complexation at pH 8.0 and relatively low ionic strength, consistent with the DFS and isothermal titration calorimetry (ITC) determinations. The findings reveal the thermodynamic and kinetic basis for binding of phosphate to SGAGKT and provide direct evidence for phosphate discrimination in phosphate/arsenate-rich environments. 2018 Journal Article http://hdl.handle.net/20.500.11937/70758 10.1021/acs.est.8b03062 American Chemical Society restricted |
| spellingShingle | Zhai, H. Qin, L. Zhang, W. Putnis, Christine Wang, L. Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title | Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title_full | Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title_fullStr | Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title_full_unstemmed | Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title_short | Dynamics and Molecular Mechanism of Phosphate Binding to a Biomimetic Hexapeptide |
| title_sort | dynamics and molecular mechanism of phosphate binding to a biomimetic hexapeptide |
| url | http://hdl.handle.net/20.500.11937/70758 |