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Area of Science:

  • Supramolecular chemistry
  • Materials science
  • Biophysics

Background:

  • Rippled beta-sheets are promising for peptide hydrogel design.
  • High-resolution structural data on these motifs in hydrogels is lacking.
  • Understanding molecular interactions is key to harnessing their potential.

Purpose of the Study:

  • To develop a molecular design strategy for studying rippled beta-sheets in peptide hydrogels.
  • To enable high-resolution structural analysis of these self-assembled materials.
  • To uncover new molecular interactions for advanced hydrogel design.

Main Methods:

  • Molecular design of enantiomeric gel-forming peptides.
  • Peptide truncation, cyclization, and Cα-methylation.
  • X-ray crystallography for structural determination.

Main Results:

  • Mirror-image macrocyclic peptides were synthesized.
  • Enantiomeric macrocycles coassembled into racemic fibril-like structures.
  • Crystallography revealed alternating enantiopure beta-hairpin blocks forming canonical and rippled beta-sheets.

Conclusions:

  • The study provides the first crystallographic evidence of parallel rippled beta-sheets.
  • New molecular interactions were identified for peptide hydrogel design.
  • This work advances the rational design of next-generation peptide hydrogels.