Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity
Physiochemical properties of engineered nanoparticles (NPs) play a vital role in nano-bio interactions, which are critical for nanotoxicity and nanomedicine research. To understand the effects of NP hydrophobicity on the formation of the protein corona, we synthesized four gold NPs with a continuous...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-03-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fbioe.2020.00210/full |
| _version_ | 1819110499845931008 |
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| author | Qianhui Yu Linxia Zhao Congcong Guo Bing Yan Bing Yan Gaoxing Su |
| author_facet | Qianhui Yu Linxia Zhao Congcong Guo Bing Yan Bing Yan Gaoxing Su |
| author_sort | Qianhui Yu |
| collection | DOAJ |
| description | Physiochemical properties of engineered nanoparticles (NPs) play a vital role in nano-bio interactions, which are critical for nanotoxicity and nanomedicine research. To understand the effects of NP hydrophobicity on the formation of the protein corona, we synthesized four gold NPs with a continuous change in hydrophobicity ranging from −2.6 to 2.4. Hydrophobic NPs adsorbed 2.1-fold proteins compared to hydrophilic ones. Proteins with small molecular weights (<50 kDa) and negatively charge (PI < 7) constituted the majority of the protein corona, especially for hydrophobic NPs. Moreover, proteins preferred binding to hydrophilic NPs (vitronectin and antithrombin III), hydrophobic NPs (serum albumin and hemoglobin fetal subunit beta), and medium hydrophobic NPs (talin 1 and prothrombin) were identified. Besides, proteins such as apolipoprotein bound to all NPs, did not show surface preference. We also found that there was a dynamic exchange between hard protein corona and solution proteins. Because of such dynamic exchanges, protein-bound NPs could expose their surface in biological systems. Hydrophilic NPs exhibited higher protein exchange rate than hydrophobic NPs. Above understandings have improved our capabilities to modulate protein corona formation by controlling surface chemistry of NPs. These will also help modulate nanotoxicity and develop better nanomedcines. |
| first_indexed | 2024-12-22T03:42:42Z |
| format | Article |
| id | doaj.art-09cd67ebdfd747afab6ed246a6ac4328 |
| institution | Directory Open Access Journal |
| issn | 2296-4185 |
| language | English |
| last_indexed | 2024-12-22T03:42:42Z |
| publishDate | 2020-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj.art-09cd67ebdfd747afab6ed246a6ac43282022-12-21T18:40:12ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852020-03-01810.3389/fbioe.2020.00210522931Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle HydrophobicityQianhui Yu0Linxia Zhao1Congcong Guo2Bing Yan3Bing Yan4Gaoxing Su5School of Environmental Science and Engineering, Shandong University, Qingdao, ChinaSchool of Pharmacy, Nantong University, Nantong, ChinaSchool of Environmental Science and Engineering, Shandong University, Qingdao, ChinaSchool of Environmental Science and Engineering, Shandong University, Qingdao, ChinaKey Laboratory for Water Quality and Conservation of the Pearl River Delta, Institute of Environmental Research at Greater Bay, Ministry of Education, Guangzhou University, Guangzhou, ChinaSchool of Pharmacy, Nantong University, Nantong, ChinaPhysiochemical properties of engineered nanoparticles (NPs) play a vital role in nano-bio interactions, which are critical for nanotoxicity and nanomedicine research. To understand the effects of NP hydrophobicity on the formation of the protein corona, we synthesized four gold NPs with a continuous change in hydrophobicity ranging from −2.6 to 2.4. Hydrophobic NPs adsorbed 2.1-fold proteins compared to hydrophilic ones. Proteins with small molecular weights (<50 kDa) and negatively charge (PI < 7) constituted the majority of the protein corona, especially for hydrophobic NPs. Moreover, proteins preferred binding to hydrophilic NPs (vitronectin and antithrombin III), hydrophobic NPs (serum albumin and hemoglobin fetal subunit beta), and medium hydrophobic NPs (talin 1 and prothrombin) were identified. Besides, proteins such as apolipoprotein bound to all NPs, did not show surface preference. We also found that there was a dynamic exchange between hard protein corona and solution proteins. Because of such dynamic exchanges, protein-bound NPs could expose their surface in biological systems. Hydrophilic NPs exhibited higher protein exchange rate than hydrophobic NPs. Above understandings have improved our capabilities to modulate protein corona formation by controlling surface chemistry of NPs. These will also help modulate nanotoxicity and develop better nanomedcines.https://www.frontiersin.org/article/10.3389/fbioe.2020.00210/fullsurface chemistryhydrophobicityprotein coronananoparticlesnano-bio interactions |
| spellingShingle | Qianhui Yu Linxia Zhao Congcong Guo Bing Yan Bing Yan Gaoxing Su Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity Frontiers in Bioengineering and Biotechnology surface chemistry hydrophobicity protein corona nanoparticles nano-bio interactions |
| title | Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity |
| title_full | Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity |
| title_fullStr | Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity |
| title_full_unstemmed | Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity |
| title_short | Regulating Protein Corona Formation and Dynamic Protein Exchange by Controlling Nanoparticle Hydrophobicity |
| title_sort | regulating protein corona formation and dynamic protein exchange by controlling nanoparticle hydrophobicity |
| topic | surface chemistry hydrophobicity protein corona nanoparticles nano-bio interactions |
| url | https://www.frontiersin.org/article/10.3389/fbioe.2020.00210/full |
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