Methodology of stable peptide based on propargylated sulfonium
Peptides can be used as effective molecular tool for covalent modification of proteins and play important roles in ligand directed covalent modification. Tyr-selective protein modifications exert a profound impact on protein functionality. Here, we developed a general strategy that involves nucleoph...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-09-01
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| Series: | Biochemistry and Biophysics Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580823000894 |
| _version_ | 1797660323194339328 |
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| author | Heng Li Zhanfeng Hou Yuena Wang Ziyuan Zhou Jin Cai Qilei Xin Feng Yin Zigang Li Naihan Xu |
| author_facet | Heng Li Zhanfeng Hou Yuena Wang Ziyuan Zhou Jin Cai Qilei Xin Feng Yin Zigang Li Naihan Xu |
| author_sort | Heng Li |
| collection | DOAJ |
| description | Peptides can be used as effective molecular tool for covalent modification of proteins and play important roles in ligand directed covalent modification. Tyr-selective protein modifications exert a profound impact on protein functionality. Here, we developed a general strategy that involves nucleophilic addition of alkyne for tyrosine modification. The terminal alkyne of propargyl sulfonium is motivated by the sulfonium center to react with phenolic hydroxyl. This approach provides a straightforward method for tyrosine modification due to its high yield in aqueous solution at physiological temperature. In addition, cyclic peptides could be obtained via adjusting pH to 8.0 from peptides consisting of tyrosine and methionine modified by propargyl bromide, and the resulting cyclic peptides are proved to have better stability, excellent 2-mercaptopyridine resistance and improved cellular uptakes. Furthermore, molecules made from the propargylated sulfonium have the potential to be used as warheads against tyrosine containing biomolecules. Collectively, we develop a direct and uncomplicated technique for modifying tyrosine residues, the strategy concerned can be widely utilized to construct stable peptides and biomolecules imaging. |
| first_indexed | 2024-03-11T18:28:06Z |
| format | Article |
| id | doaj.art-937b0015d9dd4762a5717ca2a376af74 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-03-11T18:28:06Z |
| publishDate | 2023-09-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-937b0015d9dd4762a5717ca2a376af742023-10-13T13:54:54ZengElsevierBiochemistry and Biophysics Reports2405-58082023-09-0135101508Methodology of stable peptide based on propargylated sulfoniumHeng Li0Zhanfeng Hou1Yuena Wang2Ziyuan Zhou3Jin Cai4Qilei Xin5Feng Yin6Zigang Li7Naihan Xu8State Key Laboratory of Chemical Oncogenomics, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, ChinaPingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, 518055, ChinaState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, 518055, ChinaState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, 518055, ChinaInstitute of Biopharmaceutical and Health Engineering, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, ChinaState Key Laboratory of Chemical Oncogenomics, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, ChinaState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, 518055, China; Pingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, 518055, ChinaState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, 518055, China; Pingshan Translational Medicine Center, Shenzhen Bay Laboratory, Shenzhen, 518055, China; Corresponding author. State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, 518055, China.State Key Laboratory of Chemical Oncogenomics, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, China; Institute of Biopharmaceutical and Health Engineering, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, China; Corresponding author. State Key Laboratory of Chemical Oncogenomics, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, 518055, China.Peptides can be used as effective molecular tool for covalent modification of proteins and play important roles in ligand directed covalent modification. Tyr-selective protein modifications exert a profound impact on protein functionality. Here, we developed a general strategy that involves nucleophilic addition of alkyne for tyrosine modification. The terminal alkyne of propargyl sulfonium is motivated by the sulfonium center to react with phenolic hydroxyl. This approach provides a straightforward method for tyrosine modification due to its high yield in aqueous solution at physiological temperature. In addition, cyclic peptides could be obtained via adjusting pH to 8.0 from peptides consisting of tyrosine and methionine modified by propargyl bromide, and the resulting cyclic peptides are proved to have better stability, excellent 2-mercaptopyridine resistance and improved cellular uptakes. Furthermore, molecules made from the propargylated sulfonium have the potential to be used as warheads against tyrosine containing biomolecules. Collectively, we develop a direct and uncomplicated technique for modifying tyrosine residues, the strategy concerned can be widely utilized to construct stable peptides and biomolecules imaging.http://www.sciencedirect.com/science/article/pii/S2405580823000894SulfoniumTyrosine modificationStaple peptideLabeling |
| spellingShingle | Heng Li Zhanfeng Hou Yuena Wang Ziyuan Zhou Jin Cai Qilei Xin Feng Yin Zigang Li Naihan Xu Methodology of stable peptide based on propargylated sulfonium Biochemistry and Biophysics Reports Sulfonium Tyrosine modification Staple peptide Labeling |
| title | Methodology of stable peptide based on propargylated sulfonium |
| title_full | Methodology of stable peptide based on propargylated sulfonium |
| title_fullStr | Methodology of stable peptide based on propargylated sulfonium |
| title_full_unstemmed | Methodology of stable peptide based on propargylated sulfonium |
| title_short | Methodology of stable peptide based on propargylated sulfonium |
| title_sort | methodology of stable peptide based on propargylated sulfonium |
| topic | Sulfonium Tyrosine modification Staple peptide Labeling |
| url | http://www.sciencedirect.com/science/article/pii/S2405580823000894 |
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