Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity
Abstract Amyloid-like assembly is not only associated with pathological events, but also leads to the development of novel nanomaterials with unique properties. Herein, using Fmoc diphenylalanine peptide (Fmoc–F–F) as a minimalistic model, we found that histidine can modulate the assembly behavior o...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-41591-1 |
| _version_ | 1797558073056821248 |
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| author | Ye Yuan Lei Chen Lingfei Kong Lingling Qiu Zhendong Fu Minmin Sun Yuan Liu Miaomiao Cheng Saiyu Ma Xiaonan Wang Changhui Zhao Jing Jiang Xinzheng Zhang Liping Wang Lizeng Gao |
| author_facet | Ye Yuan Lei Chen Lingfei Kong Lingling Qiu Zhendong Fu Minmin Sun Yuan Liu Miaomiao Cheng Saiyu Ma Xiaonan Wang Changhui Zhao Jing Jiang Xinzheng Zhang Liping Wang Lizeng Gao |
| author_sort | Ye Yuan |
| collection | DOAJ |
| description | Abstract Amyloid-like assembly is not only associated with pathological events, but also leads to the development of novel nanomaterials with unique properties. Herein, using Fmoc diphenylalanine peptide (Fmoc–F–F) as a minimalistic model, we found that histidine can modulate the assembly behavior of Fmoc–F–F and induce enzyme-like catalysis. Specifically, the presence of histidine rearranges the β structure of Fmoc–F–F to assemble nanofilaments, resulting in the formation of active site to mimic peroxidase-like activity that catalyzes ROS generation. A similar catalytic property is also observed in Aβ assembled filaments, which is correlated with the spatial proximity between intermolecular histidine and F-F. Notably, the assembled Aβ filaments are able to induce cellular ROS elevation and damage neuron cells, providing an insight into the pathological relationship between Aβ aggregation and Alzheimer’s disease. These findings highlight the potential of histidine as a modulator in amyloid-like assembly of peptide nanomaterials exerting enzyme-like catalysis. |
| first_indexed | 2024-03-10T17:25:17Z |
| format | Article |
| id | doaj.art-5ec1a6ff13bb4a5d9a49f8f142acbd34 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-10T17:25:17Z |
| publishDate | 2023-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-5ec1a6ff13bb4a5d9a49f8f142acbd342023-11-20T10:11:27ZengNature PortfolioNature Communications2041-17232023-09-0114111210.1038/s41467-023-41591-1Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activityYe Yuan0Lei Chen1Lingfei Kong2Lingling Qiu3Zhendong Fu4Minmin Sun5Yuan Liu6Miaomiao Cheng7Saiyu Ma8Xiaonan Wang9Changhui Zhao10Jing Jiang11Xinzheng Zhang12Liping Wang13Lizeng Gao14Key Laboratory for Molecular Enzymology and Engineering, School of Life Sciences, Jilin UniversityCAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesKey Laboratory of Animal Genetics and Breeding and Molecular Design of Jiangsu Province, Yangzhou UniversityKey Laboratory for Molecular Enzymology and Engineering, School of Life Sciences, Jilin UniversityCAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNanozyme Medical Center, School of Basic Medical Sciences, Zhengzhou UniversityNanozyme Medical Center, School of Basic Medical Sciences, Zhengzhou UniversityNanozyme Medical Center, School of Basic Medical Sciences, Zhengzhou UniversityCAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesKey Laboratory for Molecular Enzymology and Engineering, School of Life Sciences, Jilin UniversityCAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesKey Laboratory for Molecular Enzymology and Engineering, School of Life Sciences, Jilin UniversityCAS Engineering Laboratory for Nanozyme, Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesAbstract Amyloid-like assembly is not only associated with pathological events, but also leads to the development of novel nanomaterials with unique properties. Herein, using Fmoc diphenylalanine peptide (Fmoc–F–F) as a minimalistic model, we found that histidine can modulate the assembly behavior of Fmoc–F–F and induce enzyme-like catalysis. Specifically, the presence of histidine rearranges the β structure of Fmoc–F–F to assemble nanofilaments, resulting in the formation of active site to mimic peroxidase-like activity that catalyzes ROS generation. A similar catalytic property is also observed in Aβ assembled filaments, which is correlated with the spatial proximity between intermolecular histidine and F-F. Notably, the assembled Aβ filaments are able to induce cellular ROS elevation and damage neuron cells, providing an insight into the pathological relationship between Aβ aggregation and Alzheimer’s disease. These findings highlight the potential of histidine as a modulator in amyloid-like assembly of peptide nanomaterials exerting enzyme-like catalysis.https://doi.org/10.1038/s41467-023-41591-1 |
| spellingShingle | Ye Yuan Lei Chen Lingfei Kong Lingling Qiu Zhendong Fu Minmin Sun Yuan Liu Miaomiao Cheng Saiyu Ma Xiaonan Wang Changhui Zhao Jing Jiang Xinzheng Zhang Liping Wang Lizeng Gao Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity Nature Communications |
| title | Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity |
| title_full | Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity |
| title_fullStr | Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity |
| title_full_unstemmed | Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity |
| title_short | Histidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity |
| title_sort | histidine modulates amyloid like assembly of peptide nanomaterials and confers enzyme like activity |
| url | https://doi.org/10.1038/s41467-023-41591-1 |
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