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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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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...

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Updated: Oct 24, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

Electrochemically Enabled C-Terminal Peptide Modifications.

Yutong Lin¹, Lara R Malins²

¹Research School of Chemistry, Australian National University, Canberra, ACT, Australia.

Methods in Molecular Biology (Clifton, N.J.)

|August 13, 2021

Summary

This summary is machine-generated.

This study presents a simple electrochemical method for modifying peptides at their C-terminus. This technique allows for the rapid synthesis of custom peptides for various applications, including therapeutics and chemical biology.

Keywords:

Anodic oxidation C-terminal modification Decarboxylation Electroorganic synthesis Peptide modification Solid-phase peptide synthesis

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Published on: September 28, 2022

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Area of Science:

Organic Chemistry
Peptide Chemistry
Electrochemistry

Background:

Modified peptides are crucial for developing new therapeutics, chemical biology tools, and functional materials.
Efficient synthetic routes for creating designer peptides are highly sought after.

Purpose of the Study:

To detail a straightforward electrochemical method for direct C-terminal peptide modification.
To demonstrate the versatility of this approach for generating functionalized peptides.

Main Methods:

Direct anodic oxidation of C-terminal peptide carboxylic acids.
Electrochemical decarboxylation to form an N,O-acetal intermediate.
Nucleophilic engagement with the intermediate for C-terminal functionalization.

Main Results:

An operationally simple electrochemical strategy for C-terminal peptide modification was established.
Protocols for C-terminal arylation and sulfonylation were successfully developed.
The method enables the preparation of valuable functionalized peptides.

Conclusions:

This electrochemical approach offers a rapid and efficient route to designer peptides.
The method is valuable for synthesizing functionalized peptides for diverse applications.
The direct modification of native peptide sequences is achieved.