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学者姓名：陈发杰
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Abstract ：
随着新型多肽药物开发领域的迅猛发展,天然多肽的化学修饰技术备受关注.与传统化学方法相比,有机电化学方法具有条件温和、化学选择性高、原子经济性好等诸多优点,符合绿色化学理念,已广泛应用于有机合成.近年来,该方法在复杂多肽修饰中的应用优势逐步显现.本文介绍了天然多肽的电化学修饰领域的最新进展,重点讨论了相关的实验方法、反应机理以及合成应用.
Keyword ：
反应机理 反应机理 电化学 电化学 绿色化学 绿色化学 肽 肽
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| GB/T 7714 | 林子涵 , 林婉真 , 陈发杰 . 天然多肽的电化学修饰 [J]. | 大学化学 , 2025 , 40 (3) : 318-327 . |
| MLA | 林子涵 等. "天然多肽的电化学修饰" . | 大学化学 40 . 3 (2025) : 318-327 . |
| APA | 林子涵 , 林婉真 , 陈发杰 . 天然多肽的电化学修饰 . | 大学化学 , 2025 , 40 (3) , 318-327 . |
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Peptide stapling has emerged as a valuable approach for modulating peptide structures and enhancing their functional properties, with broad applications for drug discovery and biomolecular engineering. Among the diverse stapling strategies, polyfluorinated reagent-mediated approaches stand out due to their unique ability to provide desirable physicochemical properties such as improved stability, lipophilicity, and binding affinity. This review highlights recent advancements in polyfluorinated reagents for native peptide stapling, focusing on three major classes: arylation, vinylation, and amidation reagents. These reagents enable precise peptide modifications by leveraging the reactivity and selectivity modulated by fluorine substituents, facilitating the engineering of native peptides and biologics.
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| GB/T 7714 | Lin, Wanzhen , Ding, Xin , Han, Jun-Wei et al. Polyfluorinated reagents for peptide stapling [J]. | ORGANIC CHEMISTRY FRONTIERS , 2025 , 12 (8) : 2777-2789 . |
| MLA | Lin, Wanzhen et al. "Polyfluorinated reagents for peptide stapling" . | ORGANIC CHEMISTRY FRONTIERS 12 . 8 (2025) : 2777-2789 . |
| APA | Lin, Wanzhen , Ding, Xin , Han, Jun-Wei , Yu, Li-Shuang , Chen, Fa-Jie . Polyfluorinated reagents for peptide stapling . | ORGANIC CHEMISTRY FRONTIERS , 2025 , 12 (8) , 2777-2789 . |
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Introducing glycans represents an efficient chemical approach to improve the pharmacological properties of therapeutic biomolecules. Herein, we report an efficient synthesis of glycoconjugates through chlorooxime-thiol conjugation. The reactive glycosyl chlorooximes, derived from pyranoses or furanoses, readily couple to a wide range of thiol-containing substrates, including peptides, sugars, and thiophenols. This method features mild reaction conditions and fast kinetics. Capability for aqueous media and gram-scale synthesis demonstrates the potential of this method in the bioconjugation of saccharides with biologically active molecules.
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| GB/T 7714 | Gu, Wang , Huang, Jingrong , Lu, Yichi et al. Synthesis of Glycoconjugates through Chlorooxime-Thiol Conjugation [J]. | JOURNAL OF ORGANIC CHEMISTRY , 2024 , 89 (9) : 6364-6370 . |
| MLA | Gu, Wang et al. "Synthesis of Glycoconjugates through Chlorooxime-Thiol Conjugation" . | JOURNAL OF ORGANIC CHEMISTRY 89 . 9 (2024) : 6364-6370 . |
| APA | Gu, Wang , Huang, Jingrong , Lu, Yichi , Lin, Wanzhen , Xu, Wei , Chen, Fa-Jie . Synthesis of Glycoconjugates through Chlorooxime-Thiol Conjugation . | JOURNAL OF ORGANIC CHEMISTRY , 2024 , 89 (9) , 6364-6370 . |
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Abstract ：
Correction for 'Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids' by Junjie Ying et al., Org. Chem. Front., 2024, 11, 53-59, https://doi.org/10.1039/D3QO01534C.
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| GB/T 7714 | Ying, Junjie , Huang, Jingrong , Liu, Chenguang et al. Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids (vol 11, pg 53, 2024) [J]. | ORGANIC CHEMISTRY FRONTIERS , 2024 , 11 (8) : 2418-2418 . |
| MLA | Ying, Junjie et al. "Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids (vol 11, pg 53, 2024)" . | ORGANIC CHEMISTRY FRONTIERS 11 . 8 (2024) : 2418-2418 . |
| APA | Ying, Junjie , Huang, Jingrong , Liu, Chenguang , Chen, Fa-Jie , Xu, Chunfa , Chen, Fen-Er . Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids (vol 11, pg 53, 2024) . | ORGANIC CHEMISTRY FRONTIERS , 2024 , 11 (8) , 2418-2418 . |
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Peptide stapling has traditionally relied on the incorporation of unnatural amino acids and symmetric stapling. A recent article targets a typically inert C-H bond within the serine side chain, offering new avenues for conformational control and side chain engineering.
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| GB/T 7714 | Chen, Fa-Jie . Another side of side chains [J]. | NATURE REVIEWS CHEMISTRY , 2024 , 8 (6) : 406-407 . |
| MLA | Chen, Fa-Jie . "Another side of side chains" . | NATURE REVIEWS CHEMISTRY 8 . 6 (2024) : 406-407 . |
| APA | Chen, Fa-Jie . Another side of side chains . | NATURE REVIEWS CHEMISTRY , 2024 , 8 (6) , 406-407 . |
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Stapling has emerged as a powerful technique in peptide chemistry. It enables precise control over peptide conformation leading to enhanced properties such as improved stability and enhanced binding affinity. Although symmetric stapling methods have been extensively explored, the field of non-symmetric stapling of native peptides has received less attention, largely as a result of the formidable challenges it poses - in particular the complexities involved in achieving the high chemo-selectivity and site-selectivity required to simultaneously modify distinct proteinogenic residues. Over the past 5 years, there have been significant breakthroughs in addressing these challenges. In this Review, we describe the latest strategies for non-symmetric stapling of native peptides, elucidating the protocols, reaction mechanisms and underlying design principles. We also discuss current challenges and opportunities this field offers for future applications, such as ligand discovery and peptide-based therapeutics. Peptide stapling is a powerful technique used to lock peptide conformations and modulate peptide functions. This Review highlights the newest development in non-symmetric stapling of native peptides bearing natural amino acids, elucidating current advances, challenges and future opportunities. Peptide conformation has a crucial role for its functions.Non-symmetric stapling of native peptides constrains peptide conformation by covalently crosslinking two different natural residue side chains within peptides.Non-symmetric stapling can be achieved with high chemo-selectivity and site-selectivity through directing strategy or cooperative strategy.Non-symmetric stapling of native peptides holds great potential for peptide-based therapeutics.The field of non-symmetric stapling of native peptides is still in its early stages with many opportunities for improvement.
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| GB/T 7714 | Chen, Fa-Jie , Lin, Wanzhen , Chen, Fen-Er . Non-symmetric stapling of native peptides [J]. | NATURE REVIEWS CHEMISTRY , 2024 , 8 (5) : 304-318 . |
| MLA | Chen, Fa-Jie et al. "Non-symmetric stapling of native peptides" . | NATURE REVIEWS CHEMISTRY 8 . 5 (2024) : 304-318 . |
| APA | Chen, Fa-Jie , Lin, Wanzhen , Chen, Fen-Er . Non-symmetric stapling of native peptides . | NATURE REVIEWS CHEMISTRY , 2024 , 8 (5) , 304-318 . |
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Peptide therapeutics have gained great interest due to their multiple advantages over small molecule and antibody-based drugs. Peptide drugs are easier to synthesize, have the potential for oral bioavailability, and are large enough to target protein-protein interactions that are undruggable by small molecules. However, two major limitations have made it difficult to develop novel peptide therapeutics not derived from natural products, including the metabolic instability of peptides and the difficulty of reaching antibody-like potencies and specificities. Compared to linear and disulfide-monocyclized peptides, multicyclic peptides can provide increased conformational rigidity, enhanced metabolic stability, and higher potency in inhibiting protein-protein interactions. The identification of novel multicyclic peptide binders can be difficult, however, recent advancements in the construction of multicyclic phage libraries have greatly advanced the process of identifying novel multicyclic peptide binders for therapeutically relevant protein targets. This review will describe the current approaches used to create multicyclic peptide libraries, highlighting the novel chemistries developed and the proof-of-concept work done on validating these libraries against different protein targets. Multicyclic peptides are appealing for drug discovery due to their increased potency in inhibiting protein-protein interactions. This review summarizes the heretofore-reported strategies used for the construction of multicyclic phage display libraries. The multicyclization methods applicable to phage include disulfide bond formation, multi-cysteine crosslinking, and crosslinking of cysteine and non-cysteine residues. We also highlight herein the exemplary ligands for therapeutically important proteins discovered through the use of multicyclic phage libraries.+ image
Keyword ：
cyclic peptide cyclic peptide cysteine cysteine ligand discovery ligand discovery multicyclization multicyclization phage display phage display
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| GB/T 7714 | Chen, Fa-Jie , Pinnette, Nicole , Gao, Jianmin . Strategies for the Construction of Multicyclic Phage Display Libraries [J]. | CHEMBIOCHEM , 2024 , 25 (9) . |
| MLA | Chen, Fa-Jie et al. "Strategies for the Construction of Multicyclic Phage Display Libraries" . | CHEMBIOCHEM 25 . 9 (2024) . |
| APA | Chen, Fa-Jie , Pinnette, Nicole , Gao, Jianmin . Strategies for the Construction of Multicyclic Phage Display Libraries . | CHEMBIOCHEM , 2024 , 25 (9) . |
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Transition metal-mediated S-arylation has emerged as a powerful tool for the synthesis of S-arylcysteine and S-arylpeptide, which are useful building blocks in pharmacophores and biomolecules. In contrast, the catalytic protocols for arylation remain unexplored, particularly methods employing abundant metal catalysts (e.g. Cu and Ni). Herein, we reported the copper-catalyzed arylation chemistry of S-tosyl peptides with readily available arylboronic acids. This method features excellent yields and a wide variety of aryl groups, enabling the efficient synthesis of S-arylated cysteines and peptides under mild reaction conditions (room temperature, weak base). The reaction can be carried out in both batch and flow, demonstrating its utility in organic synthesis.
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| GB/T 7714 | Ying, Junjie , Huang, Jingrong , Liu, Chenguang et al. Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids [J]. | ORGANIC CHEMISTRY FRONTIERS , 2023 , 11 (1) : 53-59 . |
| MLA | Ying, Junjie et al. "Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids" . | ORGANIC CHEMISTRY FRONTIERS 11 . 1 (2023) : 53-59 . |
| APA | Ying, Junjie , Huang, Jingrong , Liu, Chenguang , Chen, Fa-Jie , Xu, Chunfa , Chen, Fen-Er . Cu-catalyzed arylation of S-tosyl peptides with arylboronic acids . | ORGANIC CHEMISTRY FRONTIERS , 2023 , 11 (1) , 53-59 . |
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