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HDX-MS of alpha-synuclein oligomers

ABSTRACT: Here we have used HDX-MS to investigate the change in structure/dynamics in synuclein oligomers formed under different conditions.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Antonio Calabrese

LAB HEAD: Sheena Radford

PROVIDER: PXD038573 | Pride | 2024-05-24

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	HDXSalvaRepeat_New.DnX	Other
	bsejb_220629_01.raw.zip	Raw
	bsejb_220629_03.raw.zip	Raw
	bsejb_220629_05.raw.zip	Raw
	bsejb_220629_07.raw.zip	Raw

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Publications

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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