Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial
Abstract Since its recent successful synthesis and due to its promising physical and chemical properties, the carbon nitrite nanomaterial, C3N3, has attracted considerable attention in various scientific areas. However, thus far, little effort has been devoted to investigating the structural influen...
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| Format: | Article |
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Nature Portfolio
2023-08-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-41125-1 |
| _version_ | 1797576793629130752 |
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| author | Yuqi Luo Zonglin Gu Jose Manuel Perez-Aguilar Weihua Liao Yiwen Huang Yanbo Luo |
| author_facet | Yuqi Luo Zonglin Gu Jose Manuel Perez-Aguilar Weihua Liao Yiwen Huang Yanbo Luo |
| author_sort | Yuqi Luo |
| collection | DOAJ |
| description | Abstract Since its recent successful synthesis and due to its promising physical and chemical properties, the carbon nitrite nanomaterial, C3N3, has attracted considerable attention in various scientific areas. However, thus far, little effort has been devoted to investigating the structural influence of the direct interaction of this 2D nanomaterial and biomolecules, including proteins and biomembranes so as to understand the physical origin of its bio-effect, particularly from the molecular landscape. Such information is fundamental to correlate to the potential nanotoxicology of the C3N3 nanomaterial. In this work, we explored the potential structural influence of a C3N3 nanosheet on the prototypical globular protein, villin headpiece (HP35) using all-atom molecular dynamics (MD) simulations. We found that HP35 could maintain its native conformations upon adsorption onto the C3N3 nanosheet regardless of the diversity in the binding sites, implying the potential advantage of C3N3 in protecting the biomolecular structure. The adsorption was mediated primarily by vdW interactions. Moreover, once adsorbed on the C3N3 surface, HP35 remains relatively fixed on the nanostructure without a distinct lateral translation, which may aid in keeping the structural integrity of the protein. In addition, the porous topological structure of C3N3 and the special water layer present on the C3N3 holes conjointly contributed to the restricted motion of HP35 via the formation of a high free energy barrier and a steric hindrance to prevent the surface displacement. This work revealed for the first time the potential influence of the 2D C3N3 nanomaterial in the protein structure and provided the corresponding in-depth molecular-level mechanism, which is valuable for future applications of C3N3 in bionanomedicine. |
| first_indexed | 2024-03-10T21:58:49Z |
| format | Article |
| id | doaj.art-ccfd9ad46caa43158f40a64ea0d8e781 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-03-10T21:58:49Z |
| publishDate | 2023-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-ccfd9ad46caa43158f40a64ea0d8e7812023-11-19T13:02:49ZengNature PortfolioScientific Reports2045-23222023-08-011311910.1038/s41598-023-41125-1Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterialYuqi Luo0Zonglin Gu1Jose Manuel Perez-Aguilar2Weihua Liao3Yiwen Huang4Yanbo Luo5Department of Gastrointestinal and Hepatobiliary Surgery, Shenzhen Longhua District Central HospitalCollege of Physical Science and Technology, Yangzhou UniversitySchool of Chemical Sciences, Meritorious Autonomous University of Puebla (BUAP)Department of Radiology, Guangzhou Nansha District Maternal and Child Health HospitalDepartment of Emergency, Nansha Hospital, Guangzhou First People’s HospitalDepartment of Gastrointestinal and Hepatobiliary Surgery, Shenzhen Longhua District Central HospitalAbstract Since its recent successful synthesis and due to its promising physical and chemical properties, the carbon nitrite nanomaterial, C3N3, has attracted considerable attention in various scientific areas. However, thus far, little effort has been devoted to investigating the structural influence of the direct interaction of this 2D nanomaterial and biomolecules, including proteins and biomembranes so as to understand the physical origin of its bio-effect, particularly from the molecular landscape. Such information is fundamental to correlate to the potential nanotoxicology of the C3N3 nanomaterial. In this work, we explored the potential structural influence of a C3N3 nanosheet on the prototypical globular protein, villin headpiece (HP35) using all-atom molecular dynamics (MD) simulations. We found that HP35 could maintain its native conformations upon adsorption onto the C3N3 nanosheet regardless of the diversity in the binding sites, implying the potential advantage of C3N3 in protecting the biomolecular structure. The adsorption was mediated primarily by vdW interactions. Moreover, once adsorbed on the C3N3 surface, HP35 remains relatively fixed on the nanostructure without a distinct lateral translation, which may aid in keeping the structural integrity of the protein. In addition, the porous topological structure of C3N3 and the special water layer present on the C3N3 holes conjointly contributed to the restricted motion of HP35 via the formation of a high free energy barrier and a steric hindrance to prevent the surface displacement. This work revealed for the first time the potential influence of the 2D C3N3 nanomaterial in the protein structure and provided the corresponding in-depth molecular-level mechanism, which is valuable for future applications of C3N3 in bionanomedicine.https://doi.org/10.1038/s41598-023-41125-1 |
| spellingShingle | Yuqi Luo Zonglin Gu Jose Manuel Perez-Aguilar Weihua Liao Yiwen Huang Yanbo Luo Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial Scientific Reports |
| title | Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| title_full | Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| title_fullStr | Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| title_full_unstemmed | Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| title_short | Moderate binding of villin headpiece protein to C3N3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| title_sort | moderate binding of villin headpiece protein to c3n3 nanosheet reveals the suitable biocompatibility of this nanomaterial |
| url | https://doi.org/10.1038/s41598-023-41125-1 |
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