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Updated: Mar 21, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Simultaneous Stabilization and Multimerization of a Peptide α-Helix by Stapling Polymerization.

Young-Joo Lee1, Sanghun Han1, Yong-Beom Lim1

  • 1Department of Materials Science & Engineering, Yonsei University, 50 Yonsei-ro, Seoul, 03722, South Korea.

Macromolecular Rapid Communications
|May 11, 2016
PubMed
Summary

A new stapling polymerization method stabilizes peptide alpha-helices and creates multimeric ligands. This technique enhances biological interactions by forming peptide-polyacrylamide conjugates for advanced biomolecular studies.

Keywords:
biopolymerspeptidespolyacrylamidesstapling polymerizationα-helices

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Area of Science:

  • Biochemistry
  • Polymer Chemistry
  • Bioconjugation

Background:

  • Specific peptide conformations, particularly alpha-helices, are vital for effective biological interactions.
  • Stabilizing these conformations and creating multimeric structures can enhance ligand efficacy.

Purpose of the Study:

  • To develop a one-pot polymerization strategy for stabilizing peptide alpha-helical conformations.
  • To simultaneously construct multimeric peptide ligands using this novel method.

Main Methods:

  • Introduced 'stapling polymerization,' a radical polymerization process.
  • Utilized acryloylated peptide side chains and vinylic monomers for crosslinking.
  • Investigated i, i+7 and i, i+4 crosslinking strategies for helix stabilization.

Main Results:

  • Demonstrated that i, i+7 crosslinking effectively stabilizes the alpha-helical conformation.
  • Showcased the formation of peptide-polyacrylamide conjugates containing approximately 3-16 peptides.
  • Confirmed the method's efficiency in creating multimeric alpha-helical structures.

Conclusions:

  • Stapling polymerization offers a straightforward yet potent approach to fabricate stabilized multimeric alpha-helices.
  • This methodology holds potential for developing advanced ligands to modulate multivalent biomacromolecular interactions.