28YD

K1R - hexagonally ordered nanofibril

Summary for 28YD

• Entry DOI: 10.2210/pdb28yd/pdb
• Related: 9H7U
• EMDB information: 56959
• Descriptor: K1R hexagonally ordered nanofibril (1 entity in total)
• Functional Keywords: honey asap, amyloid, nanofibrils, protein fibril
• Biological source: synthetic construct
• Total number of polymer chains: 18
• Total formula weight: 19373.63

Authors

Mazzotta, F.,Bonnicel, F.,Lieberwirth, I.,Landfester, K. (deposition date: 2026-02-27, release date: 2026-10-21)

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 (3.7 Å)