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Synthesis aided structural determination of amyloid-?(1-15) glycopeptides, new biomarkers for Alzheimer's disease.


ABSTRACT: Unique tyrosine glycosylated amyloid-?(1-15) glycopeptides were synthesized with well-defined stereochemistry at the glycosidic linkages. Aided by these glycopeptides and tandem mass spectrometry analysis, the naturally existing amyloid-? glycopeptides, isolated from Alzheimer's disease patients, were determined to contain an ?-linked N-acetyl galactosamine at the modified tyrosine 10 residue. Glycosylation can significantly impact the properties of amyloid-? as the glycopeptide has much lower affinity for Cu(+) ions.

SUBMITTER: Wang P 

PROVIDER: S-EPMC4221429 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Synthesis aided structural determination of amyloid-β(1-15) glycopeptides, new biomarkers for Alzheimer's disease.

Wang Peng P   Nilsson Jonas J   Brinkmalm Gunnar G   Larson Göran G   Huang Xuefei X  

Chemical communications (Cambridge, England) 20141201 95


Unique tyrosine glycosylated amyloid-β(1-15) glycopeptides were synthesized with well-defined stereochemistry at the glycosidic linkages. Aided by these glycopeptides and tandem mass spectrometry analysis, the naturally existing amyloid-β glycopeptides, isolated from Alzheimer's disease patients, were determined to contain an α-linked N-acetyl galactosamine at the modified tyrosine 10 residue. Glycosylation can significantly impact the properties of amyloid-β as the glycopeptide has much lower a  ...[more]

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