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Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress th...

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress th...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_dd03b8d056964d40bab6c08d74df6acb

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

About this item

Full title

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

Publisher

Switzerland: Frontiers Research Foundation

Journal title

Frontiers in neuroscience, 2021-06, Vol.15, p.680026

Language

English

Formats

Publication information

Publisher

Switzerland: Frontiers Research Foundation

More information

Scope and Contents

Contents

The aberrant aggregation of proteins is a key molecular event in the development and progression of a wide range of neurodegenerative disorders. We have shown previously that squalamine and trodusquemine, two natural products in the aminosterol class, can modulate the aggregation of the amyloid-β peptide (Aβ) and of α-synuclein (αS), which are asso...

Alternative Titles

Full title

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_dd03b8d056964d40bab6c08d74df6acb

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_dd03b8d056964d40bab6c08d74df6acb

Other Identifiers

ISSN

1662-4548,1662-453X

E-ISSN

1662-453X

DOI

10.3389/fnins.2021.680026

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