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Peptide Bonds02:43

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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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Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Peptide Stapling Using Sonogashira Coupling.

Devki Nandan1, Susanta Kumar Behera1, Ramesh Ramapanicker1

  • 1Department of Chemistry, India Institute of Technology Kanpur, Uttar Pradesh (U.P), 208016, India.

Chembiochem : a European Journal of Chemical Biology
|March 15, 2025
PubMed
Summary
This summary is machine-generated.

This study introduces an efficient peptide stapling method using Sonogashira coupling to link amino acid residues. The resulting stapled peptides exhibit enhanced helical structures compared to their linear counterparts, advancing peptide-based therapeutics.

Keywords:
CD spectroscopyPeptidesSonogashira couplingStapled peptidesα-helix

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Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Peptide structure and function are crucial in biological systems.
  • Stabilizing peptide secondary structures can enhance therapeutic properties.
  • Existing methods for peptide modification and stabilization have limitations.

Purpose of the Study:

  • To develop an efficient method for stapling peptides.
  • To introduce conformational constraints into peptides.
  • To investigate the structural impact of peptide stapling.

Main Methods:

  • Peptide stapling via Sonogashira coupling.
  • Modification of tyrosine residues to 4-iodophenylalanine (PhI) and 4-propargyloxyphenylalanine (TyP).
  • Circular dichroism (CD) spectroscopy to compare peptide conformations.

Main Results:

  • Successful stapling of peptides at i and i+4 or i and i+7 positions.
  • Introduction of alkyne and aryl iodide functionalities through modified tyrosine residues.
  • Stapled peptides displayed a significantly more helical conformation than linear peptides.

Conclusions:

  • The reported Sonogashira coupling method provides an efficient route for peptide stapling.
  • Peptide stapling effectively induces and stabilizes helical secondary structures.
  • This technique offers a valuable tool for designing conformationally constrained peptides with potential therapeutic applications.