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Amino acids03:42

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Related Experiment Video

Updated: Mar 15, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Crosslinked Aspartic Acids as Helix-Nucleating Templates.

Hui Zhao1, Qi-Song Liu1,2, Hao Geng1

  • 1School of Chemical Biology and Biotechnology, Shenzhen Graduate School of Peking University, Shenzhen, 518055, China.

Angewandte Chemie (International Ed. in English)
|August 31, 2016
PubMed
Summary

A new helix-nucleating template using terminal aspartic acid (TD) enables peptide modification and improved drug properties. This method complements existing helix-stabilizing techniques.

Keywords:
amino acidscircular dichroismhelical structurespeptidesprotein-protein interactions

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Area of Science:

  • Biochemistry
  • Organic Chemistry
  • Molecular Biology

Background:

  • Protein secondary structure, particularly alpha-helices, is crucial for biological function.
  • Controlling and stabilizing helical structures is a key challenge in peptide and protein engineering.
  • Existing helix-nucleating strategies often involve irreversible modifications or lack versatility.

Purpose of the Study:

  • To develop a facile and versatile N-terminal helix-nucleating template.
  • To investigate the influence of tether substituents on the nucleating efficiency.
  • To demonstrate the utility of this template in constructing peptidomimetic estrogen receptor modulators (PERMs) with enhanced therapeutic properties.

Main Methods:

  • Design and synthesis of a terminal aspartic acid (TD) based helix-nucleating template.
  • Characterization using circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy.
  • Computational analysis via molecular dynamics (MD) simulations.
  • Construction and evaluation of PERMs utilizing the TD template.

Main Results:

  • The TD template effectively nucleates alpha-helix formation.
  • The nucleating effect is modulated by substituents on the side-chain-end tether.
  • The N-terminal amine remains available for further chemical modifications.
  • PERMs synthesized with this strategy exhibited improved therapeutic profiles.

Conclusions:

  • The TD template offers a facile and adaptable method for inducing and stabilizing helical structures in peptides.
  • The preserved N-terminal amine allows for diverse downstream applications, including drug development.
  • This strategy represents a valuable addition to the toolkit for helix stabilization and peptidomimetic design.