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CryoEM structural characterization of α-Synuclein Oligomers in complex with PSMa3 peptide

ABSTRACT:

SUBMITTER: Jorge Cuéllar

PROVIDER: EMPIAR-12657 | biostudies-other |

REPOSITORIES: biostudies-other

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A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion.

Santos Jaime J Cuellar Jorge J Pallarès Irantzu I Byrd Emily J EJ Lends Alons A Moro Fernando F Abdul-Shukkoor Muhammed Bilal MB Pujols Jordi J Velasco-Carneros Lorea L Sobott Frank F Otzen Daniel E DE Calabrese Antonio N AN Muga Arturo A Pedersen Jan Skov JS Loquet Antoine A Valpuesta Jose María JM Radford Sheena E SE Ventura Salvador S

Journal of the American Chemical Society 20240429 18

Oligomeric species populated during α-synuclein aggregation are considered key drivers of neurodegeneration in Parkinson's disease. However, the development of oligomer-targeting therapeutics is constrained by our limited knowledge of their structure and the molecular determinants driving their conversion to fibrils. Phenol-soluble modulin α3 (PSMα3) is a nanomolar peptide binder of α-synuclein oligomers that inhibits aggregation by blocking oligomer-to-fibril conversion. Here, we investigate th ...[more]

PMID: 38683963

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