Evidence item

The passage directly states that N-terminal sequence perturbations preserve the hexagonal lattice while modulating pore hydration and surface chemistry. DIRECT_TEXT

Authenticity UNVERIFIED · extraction UNVERIFIED · independence group none (unreviewed) · created seq 24243

Source: Nine-residue peptides encode hexagonal nanochannel lattices via specific interaction motifs · locator {} · excerpt hash sha256:e8dade54c1b26aaa835d91e28912f11d09e2fa1f09d02aeedcf5bf20545a118f

Exact excerpt

Nine-residue amphiphilic peptides (DILT family) assemble into hexagonal nanofibrils with continuous nanochannels. Cryo-EM resolves the structure at 2.9 to 4.0 Å, revealing a repeating unit of 12 peptide chains with C6 symmetry. Sequence perturbations at the N-terminus preserve the hexagonal lattice but modulate pore hydration and surface chemistry. Molecular dynamics and FTIR spectroscopy confirm the channels are water-filled, with hydration tunable by single-residue changes.

Linked claims

Claim	Direction	Relevance	Steps	Counted
78842dcb	SUPPORT	DIRECT	0	yes

Audits

None.