28XG

DIT3 nanofibril

This is a non-PDB format compatible entry.

Summary for 28XG

• Entry DOI: 10.2210/pdb28xg/pdb
• EMDB information: 56938
• Descriptor: nanofibril peptide (KVRVSQINM) (1 entity in total)
• Functional Keywords: nanofibrils, synthetic peptide, peptide origami, structural protein
• Biological source: synthetic construct
• Total number of polymer chains: 30
• Total formula weight: 32289.39

Authors

Stoyanov, N.,Schmidt, M.,Faendrich, M. (deposition date: 2026-02-26, release date: 2026-10-07)

Primary citation

Gacanin, J.,Mazzotta, F.,Baptista, L.A.,Stoyanov, N.,Schmidt, M.,Alleva, N.,Thummaraj, T.,Bonnicel, F.,Zhou, C.,Gao, L.,Munch, J.,Bonn, M.,Fandrich, M.,Lieberwirth, I.,Cortes-Huerto, R.,Landfester, K.,Weil, T.
Sequence-encoded hexagonal lattices in multichannel peptide nanofibrils.
Nature, 657:935-943, 2026

PubMed Abstract: Structural complexity in biological matter arises from molecular information that encodes supramolecular assembly across length scales. 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. Sequence-encoded amphiphilicity combines a cross-β-dimer, an inversion point and a trimeric junction to create complementary interfaces that couple lateral growth to axial stacking, yielding honeycomb lattices with continuous approximately 5-nm solvent-accessible nanochannels. Cryo-electron microscopy resolves the supramolecular architecture and shows that lattice symmetry and pore geometry are preserved across variants. Systematic perturbations establish sequence-structure rules linking residue position to supramolecular symmetry, lattice propagation and channel topology. Molecular dynamics simulations and vibrational spectroscopy show that the channels remain water accessible and show sequence-tunable hydration. These findings establish that a minimal, sequence-encoded interaction hierarchy can programme long-range supramolecular order, providing a general framework for how short peptides can encode complex, symmetry-defined architectures.

PubMed: 42778700
DOI: 10.1038/s41586-026-11016-2

Experimental method

ELECTRON MICROSCOPY (1.78 Å)