Claims

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As of snapshot 27745 under ledger-default@0.3.0.

Claim	Type	Assessment	Score	Review checks	References
The report states that N-terminal sequence perturbations preserve the DILT hexagonal lattice while modulating pore hydration and surface chemistry.	COMPARATIVE	Supported	0.8581	0 of 4	161
Cryo-electron microscopy reportedly resolved DILT fibrils at 2.9–4.0 Å, with a repeating unit of 12 peptide chains and C6 symmetry.	QUANTITATIVE	Supported	0.8808	1 of 4	139
The DILT family of nine-residue amphiphilic peptides assembles into hexagonal nanofibrils with continuous approximately 5-nm solvent-accessible channels through cross-beta-dimer, trimeric-junction, and inversion motifs.	OBSERVATIONAL	Supported	0.8581	0 of 4	124