Modulating Peptide Self-Assembly via Triblock Chiral Patterning

Area of Science:

• Supramolecular chemistry
• Biomaterials science
• Peptide self-assembly

Background:

• Peptide self-assembly relies on cohesive interactions for hierarchical structure.
• Chiral alterations, like D-amino acid substitution, significantly impact peptide assembly.
• Block heterochiral peptides introduce chiral inversions within repeating motifs.

Purpose of the Study:

• To combinatorially explore all triblock chiral patterns for the model β-sheet-forming peptide KFE12.
• To investigate how different blockwise chiral arrangements influence peptide self-assembly morphology.
• To understand the interplay between fundamental forces and chiral interfaces in peptide aggregation.

Main Methods:

• Synthesis of KFE12 peptide variants with defined triblock chiral patterns.
• Characterization of self-assembled morphologies using various analytical techniques.
• Analysis of structural differences arising from enantiomeric chiral block arrangements.

Main Results:

• Four distinct enantiomer pairs of triblock KFE12 peptides were generated.
• Each enantiomer pair exhibited unique suprastructural morphologies.
• Observed morphologies ranged from 4-nm fibrils to micron-scale aggregates.

Conclusions:

• Blockwise chiral inversions in peptides dictate unique self-assembly outcomes.
• Peptide morphology is sensitive to the spatial arrangement of intramolecular chiral interfaces.
• This work highlights the tunable nature of peptide self-assembly through controlled chirality.