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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...

Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

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Related Experiment Video

Updated: Apr 16, 2026

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

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

Published on: August 1, 2018

A two-component 'double-click' approach to peptide stapling.

Yu Heng Lau¹, Yuteng Wu¹, Peterson de Andrade¹

¹University Chemical Laboratory, University of Cambridge, Cambridge, UK.

Nature Protocols

|March 13, 2015

Summary

This summary is machine-generated.

Double-click stapling stabilizes peptides using a copper-catalyzed reaction, enhancing their bioactivity and stability. This efficient method allows modular control over peptide drug design.

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Last Updated: Apr 16, 2026

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Construction of Cyclic Cell-Penetrating Peptides for Enhanced Penetration of Biological Barriers

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Published on: September 19, 2022

Area of Science:

Chemical Biology
Medicinal Chemistry
Biotechnology

Background:

Peptide cyclization stabilizes flexible peptides into defined conformations.
Stabilized peptides exhibit enhanced biomolecular interactions and therapeutic potential.

Purpose of the Study:

To present an optimized protocol for 'double-click' stapling of peptides.
To enhance peptide binding affinity, stability, and cellular activity.

Main Methods:

Reaction of linear diazido peptides with dialkynyl linkers under Cu(I) catalysis.
Utilizing a 1,3-dialkynylbenzene linker and peptides containing azidoornithine.
Peptide purification and confirmation steps.

Main Results:

Efficient synthesis of side chain-cyclized peptides with a bis-triazole linkage.
Demonstration of modular control over peptide bioactivity through varying staple linkages.
Protocol completion in approximately 48 hours, including lyophilization.

Conclusions:

Double-click stapling is an efficient and versatile method for peptide stabilization.
This technique enhances peptide therapeutic properties, including binding affinity and stability.
The modular nature of the protocol allows for tailored peptide drug design.