2N1E

MAX1 peptide fibril

Summary for 2N1E

• Entry DOI: 10.2210/pdb2n1e/pdb
• NMR Information: BMRB: 25558
• Descriptor: MAX1 peptide (1 entity in total)
• Functional Keywords: designed peptide, hydrogel, biomaterials, amyloid-like, cross-beta, protein fibril
• Total number of polymer chains: 8
• Total formula weight: 17895.78

Authors

Nagy-Smith, K.,Moore, E.,Schneider, J.,Tycko, R. (deposition date: 2015-03-30, release date: 2015-07-29, Last modification date: 2024-10-30)

Primary citation

Nagy-Smith, K.,Moore, E.,Schneider, J.,Tycko, R.
Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.
Proc.Natl.Acad.Sci.USA, 112:9816-9821, 2015

PubMed Abstract: 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 MAX1 adopts a β-hairpin conformation and self-assembles with high fidelity into a double-layered cross-β structure. Hairpins assemble with an in-register Syn orientation within each β-sheet layer and with an Anti orientation between layers. Surprisingly, although the MAX1 fibril network is kinetically trapped, solid-state NMR data show that fibrils within this network are monomorphic and most likely represent the thermodynamic ground state. Intermolecular interactions not available in alternative structural arrangements apparently dictate this monomorphic behavior.

PubMed: 26216960
DOI: 10.1073/pnas.1509313112

Experimental method

SOLID-STATE NMR