Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species
Abstract Inside living organisms, proteins are self‐assembled into diverse 3D structures optimized for specific functions. This structure‐function relationship can be exploited to synthesize functional materials through biotemplating and depositing functional materials onto protein structures. Howev...
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| Format: | Article |
| Language: | English |
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Wiley
2025-01-01
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| Series: | Advanced Science |
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| Online Access: | https://doi.org/10.1002/advs.202406492 |
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| author | Dae‐Hyeon Song Chang Woo Song Seunghee H. Cho Tae Yoon Kwon Hoeyun Jung Ki Hyun Park Jiyun Kim Junyoung Seo Jaeyoung Yoo Minjoon Kim Gyu Rac Lee Jisung Hwang Hyuck Mo Lee Jonghwa Shin Jennifer H. Shin Yeon Sik Jung Jae‐Byum Chang |
| author_facet | Dae‐Hyeon Song Chang Woo Song Seunghee H. Cho Tae Yoon Kwon Hoeyun Jung Ki Hyun Park Jiyun Kim Junyoung Seo Jaeyoung Yoo Minjoon Kim Gyu Rac Lee Jisung Hwang Hyuck Mo Lee Jonghwa Shin Jennifer H. Shin Yeon Sik Jung Jae‐Byum Chang |
| author_sort | Dae‐Hyeon Song |
| collection | DOAJ |
| description | Abstract Inside living organisms, proteins are self‐assembled into diverse 3D structures optimized for specific functions. This structure‐function relationship can be exploited to synthesize functional materials through biotemplating and depositing functional materials onto protein structures. However, conventional biotemplating faces limitations due to the predominantly intracellular existence of proteins and associated challenges in achieving tunability while preserving functionality. In this study, Conversion to Advanced Materials via labeled Biostructures (CamBio), an integrated biotemplating platform that involves labeling target protein structures with antibodies followed by the growth of functional materials, ensuring outstanding nanostructure tunability is proposed. Protein‐derived plasmonic nanostructures created by CamBio can serve as precise quantitative tools for assessing target species is demonstrated. The assessment is achieved through highly tunable and efficient surface‐enhanced Raman spectroscopy (SERS). CamBio enables the formation of dense nanogap hot spots among metal nanoparticles, templated by diverse fibrous proteins comprising densely repeated monomers. Furthermore, iterative antibody labeling strategies to adjust the antibody density surrounding targets, amplifying the number of nanogaps and consequently improving SERS performance are employed. Finally, cell‐patterned substrates and whole meat sections as SERS substrates, confirming their easily accessible, cost‐effective, scalable preparation capabilities and dimensional tunability are incorporated. |
| format | Article |
| id | doaj-art-98f412ab793a40838f9c8e8e7f5d2b49 |
| institution | Kabale University |
| issn | 2198-3844 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advanced Science |
| spelling | doaj-art-98f412ab793a40838f9c8e8e7f5d2b492025-01-13T15:29:43ZengWileyAdvanced Science2198-38442025-01-01122n/an/a10.1002/advs.202406492Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological SpeciesDae‐Hyeon Song0Chang Woo Song1Seunghee H. Cho2Tae Yoon Kwon3Hoeyun Jung4Ki Hyun Park5Jiyun Kim6Junyoung Seo7Jaeyoung Yoo8Minjoon Kim9Gyu Rac Lee10Jisung Hwang11Hyuck Mo Lee12Jonghwa Shin13Jennifer H. Shin14Yeon Sik Jung15Jae‐Byum Chang16Department of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Mechanical Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Mechanical Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaDepartment of Materials Science and Engineering Korea Advanced Institute of Science and Technology Daejeon 34141 South KoreaAbstract Inside living organisms, proteins are self‐assembled into diverse 3D structures optimized for specific functions. This structure‐function relationship can be exploited to synthesize functional materials through biotemplating and depositing functional materials onto protein structures. However, conventional biotemplating faces limitations due to the predominantly intracellular existence of proteins and associated challenges in achieving tunability while preserving functionality. In this study, Conversion to Advanced Materials via labeled Biostructures (CamBio), an integrated biotemplating platform that involves labeling target protein structures with antibodies followed by the growth of functional materials, ensuring outstanding nanostructure tunability is proposed. Protein‐derived plasmonic nanostructures created by CamBio can serve as precise quantitative tools for assessing target species is demonstrated. The assessment is achieved through highly tunable and efficient surface‐enhanced Raman spectroscopy (SERS). CamBio enables the formation of dense nanogap hot spots among metal nanoparticles, templated by diverse fibrous proteins comprising densely repeated monomers. Furthermore, iterative antibody labeling strategies to adjust the antibody density surrounding targets, amplifying the number of nanogaps and consequently improving SERS performance are employed. Finally, cell‐patterned substrates and whole meat sections as SERS substrates, confirming their easily accessible, cost‐effective, scalable preparation capabilities and dimensional tunability are incorporated.https://doi.org/10.1002/advs.202406492biotemplatingnanomaterialsnanostructuressurface‐enhanced Raman spectroscopy (SERS) substratetunability |
| spellingShingle | Dae‐Hyeon Song Chang Woo Song Seunghee H. Cho Tae Yoon Kwon Hoeyun Jung Ki Hyun Park Jiyun Kim Junyoung Seo Jaeyoung Yoo Minjoon Kim Gyu Rac Lee Jisung Hwang Hyuck Mo Lee Jonghwa Shin Jennifer H. Shin Yeon Sik Jung Jae‐Byum Chang Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species Advanced Science biotemplating nanomaterials nanostructures surface‐enhanced Raman spectroscopy (SERS) substrate tunability |
| title | Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species |
| title_full | Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species |
| title_fullStr | Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species |
| title_full_unstemmed | Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species |
| title_short | Highly Tunable, Nanomaterial‐Functionalized Structural Templating of Intracellular Protein Structures Within Biological Species |
| title_sort | highly tunable nanomaterial functionalized structural templating of intracellular protein structures within biological species |
| topic | biotemplating nanomaterials nanostructures surface‐enhanced Raman spectroscopy (SERS) substrate tunability |
| url | https://doi.org/10.1002/advs.202406492 |
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