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TitleConformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 518, Year 2021
Publish dateMay 3, 2021
AuthorsRitobrita Chakraborty / Sandip Dey / Pallabi Sil / Simanta Sarani Paul / Dipita Bhattacharyya / Anirban Bhunia / Jayati Sengupta / Krishnananda Chattopadhyay /
PubMed AbstractThe fibrillation pathway of alpha-Synuclein, the causative protein of Parkinson's disease, encompasses transient, heterogeneous oligomeric forms whose structural understanding and link to toxicity ...The fibrillation pathway of alpha-Synuclein, the causative protein of Parkinson's disease, encompasses transient, heterogeneous oligomeric forms whose structural understanding and link to toxicity are not yet understood. We report that the addition of the physiologically-available small molecule heme at a sub-stoichiometric ratio to either monomeric or aggregated α-Syn, targets a His50 residue critical for fibril-formation and stabilizes the structurally-heterogeneous populations of aggregates into a minimally-toxic oligomeric state. Cryo-EM 3D reconstruction revealed a 'mace'-shaped structure of this monodisperse population of oligomers, which is comparable to a solid-state NMR Greek key-like motif (where the core residues are arranged in parallel in-register sheets with a Greek key topology at the C terminus) that forms the fundamental unit/kernel of protofilaments. Further structural analyses suggest that heme binding induces a distortion in the Greek key-like architecture of the mace oligomers, which impairs their further appending into protofilaments and fibrils. Additionally, our study reports a novel mechanism of prevention as well as reclamation of amyloid fibril formation by blocking an inter-protofilament His50 residue using a small molecule.
External linksCommun Biol / PubMed:33941845 / PubMed Central
MethodsEM (single particle)
Resolution8.9 - 11.0 Å
Structure data

EMDB-31004:
Heme arrested off-pathway oligomer of alpha-synuclein
Method: EM (single particle) / Resolution: 10.4 Å

EMDB-31023:
on-pathway intermediate oligomer of alpha-synuclein
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-31024:
an arrested off-pathway oligomer of alpha-synuclein upon heme treatment after fibril formation
Method: EM (single particle) / Resolution: 8.9 Å

Source
  • Homo sapiens (human)

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