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Article

Probing APP Cleavage and Amyloid-β Assembly via Synthetic MUC-Type O-Glycosylated APP Glycopeptides.

ACS chemical neuroscience - 18 Mar 2026

Vela Navarro Nancy, De Nadai Mundim Gustavo, Regmi Deepika, Boneva Ivet, Ayyalasomayajula Ramya, Vezzi Maria E, Sopo Borraez Valentina, Crowder Alexis, Coronel-Zegarra Alejandra, Shafi Hasham, Mansour Heidi M, Merk Vivian, Du Deguo, Minond Dmitriy, Cudic Maré

Abstract excerpt

Aberrant proteolytic processing of amyloid precursor protein (APP) can alter amyloid-β (Aβ) peptide trafficking, with recent studies implicating MUC1-type O-glycosylation as a modulatory factor. In this study, we synthesized native and Swedish-mutated (Lys670Asn/Met671Leu) APP glycopeptides spanning the Aβ(1-23) region, including the β- and α-secretase cleavage sites, and introduced O-GalNAc moieties at Thr663,...

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Share to Amyloid beta-Peptides
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 41738447
DOI: 10.1021/acschemneuro.5c00608

Genes

APP
ADAM10
AFM
BACE1
MUC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

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