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Literature DB >> 28880566

Divinylsulfonamides as Specific Linkers for Stapling Disulfide Bonds in Peptides.

Zhihong Li^1,2,3, Rong Huang¹, Hongtao Xu^1,2, Jiakang Chen¹, Yuexiong Zhan¹, Xianhao Zhou¹, Hongli Chen¹, Biao Jiang¹.

Abstract

A new class of N-phenyl-divinylsulfonamides which can be easily prepared have been successfully developed and utilized as efficient linkers in the field of disulfide bond modification. Functional divinylsulfonamides provide opportunities for the specific introduction of various functionalities, including affinity probes, fluorescent tags, and drugs, into peptides.

Entities: Chemical

Mesh：

Substances：

Year: 2017 PMID： 28880566 DOI： 10.1021/acs.orglett.7b02464

Source DB: PubMed Journal: Org Lett ISSN： 1523-7052 Impact factor: 6.005

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Cited

4 in total

1. Exploring the Orthogonal Chemoselectivity of 2,4,6-Trichloro-1,3,5-Triazine (TCT) as a Trifunctional Linker With Different Nucleophiles: Rules of the Game.

Authors: Anamika Sharma; Ayman El-Faham; Beatriz G de la Torre; Fernando Albericio
Journal: Front Chem Date: 2018-11-01 Impact factor: 5.221

Divinylsulfonamides as Specific Linkers for Stapling Disulfide Bonds in Peptides.

1. Exploring the Orthogonal Chemoselectivity of 2,4,6-Trichloro-1,3,5-Triazine (TCT) as a Trifunctional Linker With Different Nucleophiles: Rules of the Game.

Review 2. Using Peptidomimetics and Constrained Peptides as Valuable Tools for Inhibiting Protein⁻Protein Interactions.

3. Cysteine [2,4] Disulfide Bond as a New Modifiable Site of α-Conotoxin TxIB.

4. Structural optimization of reversible dibromomaleimide peptide stapling.