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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...

Peptidoglycan Synthesis

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...

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Updated: Apr 16, 2026

Solid Phase Synthesis of a Functionalized Bis-Peptide Using "Safety Catch" Methodology

Solid Phase Synthesis of a Functionalized Bis-Peptide Using "Safety Catch" Methodology

Published on: May 15, 2012

Solid phase protein chemical synthesis.

Laurent Raibaut¹, Ouafâa El Mahdi, Oleg Melnyk

¹Institut Pasteur de Lille, UMR CNRS 8161, Université de Lille, 59021, Lille, France.

Topics in Current Chemistry

|March 21, 2015

Summary

Solid phase peptide synthesis (SPPS) advances peptide production. New solid-phase methods enable efficient synthesis and purification of large peptides and proteins, overcoming SPPS limitations.

Area of Science:

Biochemistry
Organic Chemistry
Chemical Biology

Background:

Chemical synthesis of peptides and small proteins is crucial for research.
Solid-phase peptide synthesis (SPPS) is effective for short peptides (<50 amino acids).
Limitations of SPPS for large homogeneous peptides necessitate advanced methods.

Purpose of the Study:

To provide a comprehensive review of solid-phase methods for polypeptide production and purification.
To highlight advancements in solid-phase synthesis of large peptides and proteins.
To discuss the adaptation of native chemical ligation (NCL) to solid-phase techniques.

Main Methods:

Review of solid-phase peptide synthesis (SPPS) techniques.
Analysis of solid-phase covalent and non-covalent capture purification methods.

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Examination of native chemical ligation (NCL) adapted for solid-phase protein synthesis, including linker technologies and thioester chemistries.

Main Results:

SPPS significantly improved access to short peptides.
Development of solid-phase purification methods addresses limitations for larger peptides.
Adaptation of NCL to solid phase enables synthesis of large peptides and proteins.

Conclusions:

Solid-phase methodologies are continuously evolving for peptide and protein synthesis.
Novel linker technologies and ligation strategies enhance the production of large, homogeneous peptides and proteins.
This review covers key developments in solid-phase chemical synthesis for peptides and proteins.