Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients
Metal ions play a pivotal role in regulating and determining the functions of proteins and peptides in nature. This study aims to investigate the regulatory role of metal ions in peptide assembly and explore the influence of sequence variations and metal ions on the structure and function of resulti...
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| Format: | Article |
| Language: | English |
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KeAi Communications Co., Ltd.
2023-12-01
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| Series: | Supramolecular Materials |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667240523000107 |
| _version_ | 1797377788227878912 |
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| author | Shengtao Wang Anhe Wang Jingtao Li Qingquan Han Yafeng Jing Jieling Li Shiyu Du Peter H. Seeberger Jian Yin Shuo Bai |
| author_facet | Shengtao Wang Anhe Wang Jingtao Li Qingquan Han Yafeng Jing Jieling Li Shiyu Du Peter H. Seeberger Jian Yin Shuo Bai |
| author_sort | Shengtao Wang |
| collection | DOAJ |
| description | Metal ions play a pivotal role in regulating and determining the functions of proteins and peptides in nature. This study aims to investigate the regulatory role of metal ions in peptide assembly and explore the influence of sequence variations and metal ions on the structure and function of resulting peptide nanoarchitectures. Dipeptide sequences with distinct charged properties (positive and negative) and functional groups (-COOH, -NH2, and phenolic hydroxyl) were meticulously selected and co-assembled with various metal ions (Au3+, Ag+, and Pt4+). The findings highlight the crucial functional role of the phenolic hydroxyl group of tyrosine in metal ion reduction, while positively charged groups promote metal ion accumulation through electrostatic forces, facilitating co-assembly. The formation of ordered structures in Au@Fmoc-YK and Au@Fmoc-YR nanoarchitectures further validates the significant interaction among metal ions, tyrosine-OH, and positively charged NH2. Notably, these nanoarchitectures possess the unique attribute of being prepared under physiological conditions, specifically at 37 °C, without the need for organic solvents or chemical modifications of peptides. This approach offers a straightforward means of constructing diverse functional nanoarchitectures based on peptides and metal ions. Moreover, Au@Fmoc-YR exhibits good performance as a nanoenzyme for detecting glucose in complex bodily fluids and plasma GSH in tumor patients, showcasing its promising potential for medical applications. |
| first_indexed | 2024-03-08T19:58:30Z |
| format | Article |
| id | doaj.art-ba41357643b44f16a6d00cb0908f2668 |
| institution | Directory Open Access Journal |
| issn | 2667-2405 |
| language | English |
| last_indexed | 2024-03-08T19:58:30Z |
| publishDate | 2023-12-01 |
| publisher | KeAi Communications Co., Ltd. |
| record_format | Article |
| series | Supramolecular Materials |
| spelling | doaj.art-ba41357643b44f16a6d00cb0908f26682023-12-24T04:47:17ZengKeAi Communications Co., Ltd.Supramolecular Materials2667-24052023-12-012100040Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patientsShengtao Wang0Anhe Wang1Jingtao Li2Qingquan Han3Yafeng Jing4Jieling Li5Shiyu Du6Peter H. Seeberger7Jian Yin8Shuo Bai9State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, PR ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR ChinaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, PR ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR ChinaDepartment of Gastroenterology, China-Japan Friendship Hospital, Beijing, 100029, PR ChinaDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, Potsdam, 14476, Germany; Corresponding authors.Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, PR China; Corresponding authors.State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing, 100190, PR China; Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, 100190, PR China; Corresponding authors.Metal ions play a pivotal role in regulating and determining the functions of proteins and peptides in nature. This study aims to investigate the regulatory role of metal ions in peptide assembly and explore the influence of sequence variations and metal ions on the structure and function of resulting peptide nanoarchitectures. Dipeptide sequences with distinct charged properties (positive and negative) and functional groups (-COOH, -NH2, and phenolic hydroxyl) were meticulously selected and co-assembled with various metal ions (Au3+, Ag+, and Pt4+). The findings highlight the crucial functional role of the phenolic hydroxyl group of tyrosine in metal ion reduction, while positively charged groups promote metal ion accumulation through electrostatic forces, facilitating co-assembly. The formation of ordered structures in Au@Fmoc-YK and Au@Fmoc-YR nanoarchitectures further validates the significant interaction among metal ions, tyrosine-OH, and positively charged NH2. Notably, these nanoarchitectures possess the unique attribute of being prepared under physiological conditions, specifically at 37 °C, without the need for organic solvents or chemical modifications of peptides. This approach offers a straightforward means of constructing diverse functional nanoarchitectures based on peptides and metal ions. Moreover, Au@Fmoc-YR exhibits good performance as a nanoenzyme for detecting glucose in complex bodily fluids and plasma GSH in tumor patients, showcasing its promising potential for medical applications.http://www.sciencedirect.com/science/article/pii/S2667240523000107PeptideMetal ionsSelf-assemblySpontaneouslyBiocatalysisGlucose detecting |
| spellingShingle | Shengtao Wang Anhe Wang Jingtao Li Qingquan Han Yafeng Jing Jieling Li Shiyu Du Peter H. Seeberger Jian Yin Shuo Bai Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients Supramolecular Materials Peptide Metal ions Self-assembly Spontaneously Biocatalysis Glucose detecting |
| title | Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients |
| title_full | Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients |
| title_fullStr | Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients |
| title_full_unstemmed | Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients |
| title_short | Sequence-dependent catalysis and assembly to form peptide/Au nanoenzyme for glucose and plasma GSH detecting in cancer patients |
| title_sort | sequence dependent catalysis and assembly to form peptide au nanoenzyme for glucose and plasma gsh detecting in cancer patients |
| topic | Peptide Metal ions Self-assembly Spontaneously Biocatalysis Glucose detecting |
| url | http://www.sciencedirect.com/science/article/pii/S2667240523000107 |
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