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The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Re...

The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Re...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_576ea8a4e6754caea2b9a7ee3231ccb0

The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β

About this item

Full title

The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β

Publisher

Switzerland: MDPI AG

Journal title

Molecules (Basel, Switzerland), 2023-05, Vol.28 (10), p.4001

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

A technique to image α-synuclein (αSYN) fibrils in vivo is an unmet scientific and clinical need that would represent a transformative tool in the understanding, diagnosis, and treatment of various neurodegenerative diseases. Several classes of compounds have shown promising results as potential PET tracers, but no candidate has yet exhibited the a...

Alternative Titles

Full title

The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_576ea8a4e6754caea2b9a7ee3231ccb0

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_576ea8a4e6754caea2b9a7ee3231ccb0

Other Identifiers

ISSN

1420-3049

E-ISSN

1420-3049

DOI

10.3390/molecules28104001

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