Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation
Protein products perform important roles in the biochemistry field, but the thermal inactivation of proteins will increase the difficulty of their transport, storage and application. Therefore, improving the thermal stability of proteins has become a thorny challenge. Natural molecular chaperones ca...
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| Format: | Article |
| Language: | English |
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KeAi Communications Co., Ltd.
2024-12-01
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| Series: | Supramolecular Materials |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667240524000059 |
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| author | Shuyue Zhao Bingqiang Li Yiqing Song Shian Wu Haodong Hu Jianzu Wang Linqi Shi Fan Huang |
| author_facet | Shuyue Zhao Bingqiang Li Yiqing Song Shian Wu Haodong Hu Jianzu Wang Linqi Shi Fan Huang |
| author_sort | Shuyue Zhao |
| collection | DOAJ |
| description | Protein products perform important roles in the biochemistry field, but the thermal inactivation of proteins will increase the difficulty of their transport, storage and application. Therefore, improving the thermal stability of proteins has become a thorny challenge. Natural molecular chaperones can efficiently improve the resistance of proteins to environmental stimuli by reversible supramolecular assembly with proteins. Inspired by this machine, herein we designed a nanochaperone (nChap) with thermo-responsive amphiphilic surfaces that can prevent thermal denaturation and facilitate refolding of green fluorescent proteins (GFPs). By mimicking the hydrophobic microregion of natural chaperones, this nChap can effectively capture free GFPs and hide them into surface confined spaces, thereby shielding exposed hydrophobic sites of GFPs and preventing their irreversible thermal aggregation. When the heat stimulation disappeared, the thermosensitive segments of the nChaps underwent the hydrophilic transition, which provided suitable microenvironments for GFPs refolding. More importantly, nChaps could also actively adsorb to the surface of immobilized GFPs at high temperatures and realize the satisfactory dissociation of the nChap-protein complex upon cooling, which exhibited excellent chaperone-like activity. This work provides significant insights for understanding and developing strategies to improve protein stability. |
| format | Article |
| id | doaj-art-ce8a145fe5bf4efea72ed5dde01d4684 |
| institution | Kabale University |
| issn | 2667-2405 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Supramolecular Materials |
| spelling | doaj-art-ce8a145fe5bf4efea72ed5dde01d46842024-12-31T04:13:24ZengKeAi Communications Co., Ltd.Supramolecular Materials2667-24052024-12-013100067Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal DenaturationShuyue Zhao0Bingqiang Li1Yiqing Song2Shian Wu3Haodong Hu4Jianzu Wang5Linqi Shi6Fan Huang7State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials of Ministry of Education, College of Chemistry, Nankai University, Tianjin 300071, PR ChinaDepartment of Cardiology, Tianjin NanKai Hospital, Tianjin, 300100, PR ChinaState Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials of Ministry of Education, College of Chemistry, Nankai University, Tianjin 300071, PR ChinaState Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, Tianjin, 300071, PR ChinaState Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials of Ministry of Education, College of Chemistry, Nankai University, Tianjin 300071, PR ChinaState Key Laboratory of Separation Membranes and Membrane Processes, School of Environmental Science and Engineering, Tiangong University, Tianjin, 300387, PR China; Corresponding authors.State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Functional Polymer Materials of Ministry of Education, College of Chemistry, Nankai University, Tianjin 300071, PR China; Corresponding authors.State Key Laboratory of Advanced Medical Materials and Devices, Tianjin Key Laboratory of Radiation Medicine and Molecular Nuclear Medicine, Key Laboratory of Radiopharmacokinetics for Innovative Drugs, Tianjin Institutes of Health Science, Institute of Radiation Medicine, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin 300192, PR China; Corresponding authors.Protein products perform important roles in the biochemistry field, but the thermal inactivation of proteins will increase the difficulty of their transport, storage and application. Therefore, improving the thermal stability of proteins has become a thorny challenge. Natural molecular chaperones can efficiently improve the resistance of proteins to environmental stimuli by reversible supramolecular assembly with proteins. Inspired by this machine, herein we designed a nanochaperone (nChap) with thermo-responsive amphiphilic surfaces that can prevent thermal denaturation and facilitate refolding of green fluorescent proteins (GFPs). By mimicking the hydrophobic microregion of natural chaperones, this nChap can effectively capture free GFPs and hide them into surface confined spaces, thereby shielding exposed hydrophobic sites of GFPs and preventing their irreversible thermal aggregation. When the heat stimulation disappeared, the thermosensitive segments of the nChaps underwent the hydrophilic transition, which provided suitable microenvironments for GFPs refolding. More importantly, nChaps could also actively adsorb to the surface of immobilized GFPs at high temperatures and realize the satisfactory dissociation of the nChap-protein complex upon cooling, which exhibited excellent chaperone-like activity. This work provides significant insights for understanding and developing strategies to improve protein stability.http://www.sciencedirect.com/science/article/pii/S2667240524000059Protein refoldingChaperoneGreen fluorescent proteinThermal denaturationSelf-assembly |
| spellingShingle | Shuyue Zhao Bingqiang Li Yiqing Song Shian Wu Haodong Hu Jianzu Wang Linqi Shi Fan Huang Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation Supramolecular Materials Protein refolding Chaperone Green fluorescent protein Thermal denaturation Self-assembly |
| title | Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation |
| title_full | Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation |
| title_fullStr | Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation |
| title_full_unstemmed | Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation |
| title_short | Temperature-Responsive Self-Assembly Nanochaperone Protects Green Fluorescent Proteins from Thermal Denaturation |
| title_sort | temperature responsive self assembly nanochaperone protects green fluorescent proteins from thermal denaturation |
| topic | Protein refolding Chaperone Green fluorescent protein Thermal denaturation Self-assembly |
| url | http://www.sciencedirect.com/science/article/pii/S2667240524000059 |
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