Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.
Ontology highlight
ABSTRACT:
SUBMITTER: Nagy-Smith K
PROVIDER: S-EPMC4538636 | biostudies-literature | 2015 Aug
REPOSITORIES: biostudies-literature
Publications
Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.
Nagy-Smith Katelyn K Moore Eric E Schneider Joel J Tycko Robert R
Proceedings of the National Academy of Sciences of the United States of America 20150727 32
Most, if not all, peptide- and protein-based hydrogels formed by self-assembly can be characterized as kinetically trapped 3D networks of fibrils. The propensity of disease-associated amyloid-forming peptides and proteins to assemble into polymorphic fibrils suggests that cross-β fibrils comprising hydrogels may also be polymorphic. We use solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. We find that ...[more]
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