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Related Experiment Video

Updated: Jun 4, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

Chiral, fully extended helical peptides.

Marco Crisma1, Alessandro Moretto, Cristina Peggion

  • 1ICB, Padova Unit, CNR, Department of Chemistry, University of Padova, via Marzolo 1, 35131 Padua, Italy.

Amino Acids
|February 5, 2011
PubMed
Summary
This summary is machine-generated.

Researchers synthesized chiral homo-peptide esters and found they adopt extended helical structures (2.0(5)-helices). These unique helical peptide spacers offer the longest residue separation, advancing peptide science.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

  • Peptide Chemistry
  • Supramolecular Chemistry
  • Structural Biology

Background:

  • Chiral alpha-amino acids are building blocks for peptides with unique structural properties.
  • Homo-peptides, composed of repeating amino acid units, can adopt specific conformations.
  • Understanding peptide conformation is crucial for designing novel materials and therapeutics.

Purpose of the Study:

  • To synthesize N-protected homo-peptide esters using chiral C(α)-ethyl, C(α)-n-pentylglycine.
  • To investigate the conformational preferences of these homo-peptides in solution and solid states.
  • To evaluate the potential of these peptides as rigid helical spacers.

Main Methods:

  • Solution-phase synthesis of homo-peptide esters up to the hexapeptide level.
  • Fourier-transform infrared (FTIR) spectroscopy to analyze secondary structures.
  • Nuclear magnetic resonance (NMR) spectroscopy for structural elucidation.
  • X-ray diffraction to determine crystal structures and confirm conformations.

Main Results:

  • Successful synthesis of N-protected homo-peptide esters derived from chiral C(α)-ethyl, C(α)-n-pentylglycine.
  • Consistent adoption of fully extended helical structures, specifically 2.0(5)-helices, observed in both chloroform solution and crystal states.
  • The observed helical structures were independent of the peptide chain length (up to hexapeptide).
  • These homo-peptides exhibit the longest C(i)(α)...C(i+1)(α) separation per residue among chiral, rigid helical peptide spacers derived from alpha-amino acids.

Conclusions:

  • Chiral C(α)-ethyl, C(α)-n-pentylglycine homo-peptides predominantly form extended 2.0(5)-helical structures.
  • These peptides represent a novel class of rigid helical spacers with significant potential in biomaterials and molecular design.
  • The findings provide insights into structure-property relationships in conformationally restricted peptides.