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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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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Hydrocarbon-stapled peptides: principles, practice, and progress.

Loren D Walensky1, Gregory H Bird

  • 1Department of Pediatric Oncology, Dana-Farber Cancer Institute , Boston, Massachusetts 02215, United States.

Journal of Medicinal Chemistry
|March 8, 2014
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Summary

Researchers developed stapled peptides, which are stabilized protein structures, to improve drug discovery and create new therapeutics. This decade-long work highlights methods for creating effective stapled peptide tools and treatments.

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Protein structure is crucial for biological processes and drug discovery.
  • Peptides, particularly alpha-helices, mediate protein-protein interactions but can be unstable.
  • Stabilizing peptide structure is key for therapeutic development.

Purpose of the Study:

  • To describe the development of all-hydrocarbon stapled peptides over a decade.
  • To showcase stapled peptides as biomedical research tools and therapeutic prototypes.
  • To share lessons learned, pitfalls, and success factors in stapled peptide design.

Main Methods:

  • Incorporation of all-hydrocarbon staples to stabilize peptide alpha-helical structure.
  • Application of design and synthesis principles for enhanced peptide properties.
  • Evaluation of stapled peptides for protease resistance, cellular penetrance, and biological activity.

Main Results:

  • Stapled peptides successfully conferred stable alpha-helical structure.
  • Achieved enhanced protease resistance and cellular penetrance.
  • Demonstrated biological activity, supporting their use as research tools and therapeutics.

Conclusions:

  • Stapled peptides represent a viable strategy for stabilizing bioactive peptide structures.
  • This approach offers a promising avenue for developing novel therapeutics and research tools.
  • Decade-long experience provides valuable insights into the successful development of stapled peptides.