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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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Backbone-Constrained Tripeptides Enable Sequence Control of Solid-State Dynamics.

Kuntrapakam Hema1, Hamish W A Swanson1, Elma Naranjo1,2

  • 1Advanced Science Research Center (ASRC), The Graduate Center of the City University of New York, New York, USA.

Angewandte Chemie (International Ed. in English)
|March 4, 2026
PubMed
Summary
This summary is machine-generated.

Minimalist tripeptides with specific aromatic residues show how sequence dictates solid-state material properties. Aromatic residue type controls peptide conformation, influencing crystallization and resulting material dynamics and surface characteristics.

Keywords:
non‐covalent interactionspeptide assemblypeptide crystalssupramolecular dynamicstryptophan

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Area of Science:

  • Materials Science
  • Biomolecular Engineering
  • Chemical Physics

Background:

  • Rational design of peptide-based materials is hindered by the complex relationship between peptide sequence, supramolecular assembly, and solid-state properties.
  • Controlling peptide conformational dynamics is key to tailoring material characteristics.

Purpose of the Study:

  • To investigate how simple aromatic residue substitutions in minimalist tripeptides influence supramolecular dynamics and solid-state material properties.
  • To establish a design principle for engineering dynamic properties in peptide materials based on sequence.

Main Methods:

  • Utilized N-terminal proline to rigidify the peptide backbone in PXX tripeptides (proline, aromatic residue X).
  • Employed molecular dynamics simulations, NMR spectroscopy, and fluorescence spectroscopy to analyze peptide conformations and dynamics.
  • Performed solid-state characterization to correlate molecular dynamics with bulk material properties.

Main Results:

  • Peptides with a C-terminal tryptophan (PXW) exhibited adaptable conformations and promoted crystallization, forming stiff, dynamic, wettable crystals.
  • Peptides with a C-terminal phenylalanine (PXF) adopted restricted conformations, leading to soluble aggregates and static, hydrophobic materials.
  • Aromatic residue type (W vs. F) significantly altered peptide energy landscapes and interaction spaces, dictating assembly pathways.

Conclusions:

  • Aromatic residues are critical determinants of supramolecular assembly, crystallization behavior, and solid-state dynamics in peptide materials.
  • Sequence-encoded conformational adaptability offers a direct route for engineering dynamic and functional solid-state peptide materials.