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TitleIn cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateSep 10, 2024
AuthorsShoyab Ansari / Dominique Lagasca / Rania Dumarieh / Yiling Xiao / Sakshi Krishna / Yang Li / Kendra K Frederick /
PubMed AbstractAmyloid forms of α-synuclein adopt different conformations depending on environmental conditions. Advances in structural biology have accelerated fibril characterization. However, it remains unclear ...Amyloid forms of α-synuclein adopt different conformations depending on environmental conditions. Advances in structural biology have accelerated fibril characterization. However, it remains unclear which conformations predominate in biological settings because current methods typically not only require isolating fibrils from their native environments, but they also do not provide insight about flexible regions. To address this, we characterized α-syn amyloid seeds and used sensitivity enhanced nuclear magnetic resonance to investigate the amyloid fibrils resulting from seeded amyloid propagation in different settings. We found that the amyloid fold and conformational preferences of flexible regions are faithfully propagated and in cellular lysates. However, seeded propagation of amyloids inside cells led to the minority conformation in the seeding population becoming predominant and more ordered, and altered the conformational preferences of flexible regions. The examination of the entire ensemble of protein conformations in biological settings that is made possible with this approach may advance our understanding of protein misfolding disorders and facilitate structure-based drug design efforts.
External linksbioRxiv / PubMed:39314304 / PubMed Central
MethodsEM (helical sym.)
Resolution2.21 - 2.68 Å
Structure data

45650

9ckk

EMDB-45650, PDB-9ckk:
Cryo-EM structure of acetylated alpha-synuclein A53T fibril - polymorph A
Method: EM (helical sym.) / Resolution: 2.21 Å

45651

9ckl

EMDB-45651, PDB-9ckl:
Cryo-EM structure of acetylated alpha-synuclein A53T fibril - polymorph B
Method: EM (helical sym.) / Resolution: 2.68 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid / neurodegeneration / aggregrate

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