Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/106076
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | en_US |
dc.contributor | Research Centre for Carbon-Strategic Catalysis | en_US |
dc.creator | Lu, QY | en_US |
dc.creator | Zhang, BY | en_US |
dc.creator | Sun, MZ | en_US |
dc.creator | Lu, L | en_US |
dc.creator | Chen, BA | en_US |
dc.creator | Wong, HH | en_US |
dc.creator | Chan, CH | en_US |
dc.creator | Wu, T | en_US |
dc.creator | Huang, BL | en_US |
dc.date.accessioned | 2024-05-03T00:45:03Z | - |
dc.date.available | 2024-05-03T00:45:03Z | - |
dc.identifier.uri | http://hdl.handle.net/10397/106076 | - |
dc.language.iso | en | en_US |
dc.publisher | Cell Press | en_US |
dc.rights | © 2023 The Authors. | en_US |
dc.rights | This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | en_US |
dc.rights | The following publication Lu, Q., Zhang, B., Sun, M., Lu, L., Chen, B., Wong, H. H., Chan, C. H., Wu, T., & Huang, B. (2023). Probing the affinity of noble metal nanoparticles to the segments of the SARS-CoV-2 spike protein. iScience, 26(3), 106110 is available at https://dx.doi.org/10.1016/j.isci.2023.106110. | en_US |
dc.title | Probing the affinity of noble metal nanoparticles to the segments of the SARS-CoV-2 spike protein | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.volume | 26 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.doi | 10.1016/j.isci.2023.106110 | en_US |
dcterms.abstract | Currently, scientists have devoted great efforts to finding effective treatments to combat COVID-19 infections. Although noble metal nanoparticles are able to realize protein modifications, their interactions with the protein are still unclear from the atomic perspective. To supply a general understanding, in this work, we have carried out theoretical calculations to investigate the interaction be-tween protein segments (RBD1, RBD2, RBD3) of SARS-Cov-2 spike protein and a series of noble metal (Au, Ag, Cu, Pd, Pt) surfaces regarding the binding strength, protein orientations, and electronic modulations. In particular, the Au surface has shown the strongest binding preferences for the protein segments, which induces electron transfer between the Au and receptor-binding domain (RBD) segments. This further leads to the polarization of segments for virus dena-turation. This work has offered a direct visualization of protein interactions with noble metal surfaces from the atomic level, which will benefit anti-virus material developments in the future. | en_US |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | iScience, 17 Mar. 2023, v. 26, no. 3, 106110 | en_US |
dcterms.isPartOf | iScience | en_US |
dcterms.issued | 2023-03 | - |
dc.identifier.isi | WOS:000994873400001 | - |
dc.identifier.eissn | 2589-0042 | en_US |
dc.identifier.artn | 106110 | en_US |
dc.description.validate | 202405 bcrc | en_US |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_Scopus/WOS | - |
dc.description.fundingSource | RGC | en_US |
dc.description.fundingSource | Others | en_US |
dc.description.fundingText | National Key R&D Program of China | en_US |
dc.description.fundingText | National Natural Science Foundation of China | en_US |
dc.description.fundingText | Hong Kong Polytechnic University | en_US |
dc.description.fundingText | Departmental General Research Fund | en_US |
dc.description.fundingText | Shenzhen Fundamental Research Scheme-General Program | en_US |
dc.description.fundingText | Research Centre for Carbon-Strategic Catalysis (RC-CSC) | en_US |
dc.description.fundingText | Research Institute for Smart Energy (RISE) | en_US |
dc.description.fundingText | Research Institute for Intelligent Wearable Systems (RI-IWEAR) of the Hong Kong Polytechnic University | en_US |
dc.description.pubStatus | Published | en_US |
dc.description.oaCategory | CC | en_US |
Appears in Collections: | Journal/Magazine Article |
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File | Description | Size | Format | |
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i009_1-s2.0-S2589004223001876-main.pdf | 2.78 MB | Adobe PDF | View/Open |
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