Nature study shows nine-residue peptides self-assemble into honeycomb nanochannels

The wire

1. 01Max Planck Institute for Polymer Research and Ulm collaborators report in Nature that minimal nine-residue peptides encode lateral interaction motifs that tile into multichannel nanofibrils with roughly 5-nm solvent-accessible channels.
2. 02Systematic residue substitutions established sequence-structure rules linking position to lattice symmetry and channel topology, a design framework for engineering ordered peptide materials.
3. 03Molecular dynamics and vibrational spectroscopy indicate channel water is more tightly bound than bulk water; the work is structural and materials-focused, with no therapeutic application tested.

From the source

Sequence-encoded hexagonal lattices in multichannel peptide nanofibrils

Structural complexity in biological matter arises from molecular information that encodes supramolecular assembly across length scales 1 , 2 , 3 . Here we show that minimal nine-residue peptides can encode discrete lateral interaction motifs that direct supramolecular organization. These motifs generate hexagonal pores and hierarchically tile into multichannel nanofibrils with defined topology. Se