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Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

Preparation and Reactions of Sulfides

Preparation and Reactions of Sulfides

Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.

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Updated: Jun 16, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

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Published on: August 1, 2018

Cleavable and Cysteine-Selective Peptide Stapling Via Bifunctional Aryl Thioethers.

Wei Zhang¹, Yu-Long Li¹, Xing-Long Tan¹

¹School of Pharmaceutical Science, Hengyang Medical School, University of South China, Hengyang 421001, Hunan, China.

Organic Letters

|June 13, 2026

Summary

A new peptide stapling method uses aryl thioether derivatives for improved drug-likeness. The stapled peptides show enhanced stability and cell permeability, with a cleavable moiety for releasing native peptides, aiding peptide drug development.

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Last Updated: Jun 16, 2026

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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

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Published on: October 2, 2018

Area of Science:

Medicinal Chemistry
Drug Discovery
Bioconjugation Chemistry

Background:

Peptide stapling enhances peptide drug-likeness and stability compared to linear analogs.
Developing efficient and selective peptide stapling techniques is crucial for drug discovery.
Existing methods may have limitations in scope or cleavability.

Purpose of the Study:

To develop a novel, cleavable, and cysteine-selective peptide stapling method.
To create stapled peptides with improved drug-like properties.
To demonstrate the utility of this approach in peptide drug development.

Main Methods:

Aryl thioether derivatives were utilized for cysteine-selective peptide stapling.
The method was tested for its tolerance to various reagents and peptide sequences.
Characterization of stapled peptides included conformational analysis, stability assays, and cell permeability studies.
Cleavage of the stapling moiety was achieved using exogenous thiols.

Main Results:

The developed method efficiently produces stapled peptides.
Stapled peptides maintained stable alpha-helical conformations.
Significant improvements in chemical and enzymatic stability were observed.
Enhanced cellular membrane permeability was demonstrated for the stapled peptides.
The stapling moiety was successfully cleaved by thiols to release linear peptides.

Conclusions:

A cleavable, cysteine-selective peptide stapling approach using aryl thioether derivatives is reported.
This method yields stapled peptides with superior stability, permeability, and drug-like properties.
The cleavable nature of the stapling moiety offers a versatile tool for peptide therapeutics development.