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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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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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Structural optimization of reversible dibromomaleimide peptide stapling.

Ayanna Lindsey-Crosthwait1,2, Diana Rodriguez-Lema1,2, Martin Walko1,2

  • 1School of Chemistry, University of Leeds Leeds UK.

Peptide Science (Hoboken, N.J.)
|December 23, 2021
PubMed
Summary
This summary is machine-generated.

Researchers optimized a reversible peptide stapling method using dibromomaleimides. The best results for promoting alpha-helical structure were achieved with L-Cysteine and L-homocysteine, aiding drug discovery.

Keywords:
constrained peptidesdibromomaleimidepeptide conformationprotein‐protein interactions

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Area of Science:

  • Chemical Biology
  • Medicinal Chemistry
  • Organic Chemistry

Background:

  • Constraining peptides into alpha-helical conformations is crucial for inhibiting protein-protein interactions.
  • A novel reversible peptide stapling method using dibromomaleimides and native cysteine/homocysteine residues has been developed.
  • Optimizing this stapling strategy is key for advancing peptidomimetic drug discovery.

Purpose of the Study:

  • To optimize the dibromomaleimide-based peptide stapling methodology.
  • To investigate the kinetics of macrocyclization and helicity promotion with various thiol-containing amino acids.
  • To identify the optimal amino acid combination for effective peptide stapling.

Main Methods:

  • Utilizing a model peptide Ac-X1AAAX5-NH2 with varying thiol-containing amino acids at positions X1 and X5.
  • Focusing on the thiol-selective reactivity of dibromomaleimides for macrocyclization.
  • Analyzing the kinetics of the stapling reaction and quantifying the induced helical content.

Main Results:

  • The study identified L-Cysteine (L-Cys) at position X1 and L-homocysteine (L-hCys) at position X5 as the optimal combination.
  • This specific combination demonstrated favorable macrocyclization kinetics and significant promotion of alpha-helical structure.
  • The findings provide valuable insights into optimizing the dibromomaleimide stapling strategy.

Conclusions:

  • The optimal stapling combination of L-Cys and L-hCys enhances the utility of the dibromomaleimide method.
  • This optimized strategy can be effectively implemented in peptidomimetic ligand discovery programs.
  • Further application of this technique holds promise for developing novel therapeutics targeting protein-protein interactions.