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• W2079462340 endingPage "804" @default.
• W2079462340 startingPage "797" @default.
• W2079462340 abstract "Typical markers of protein aging are spontaneous post-translational modifications such as amino acid racemization (AAR) and amino acid isomerization (AAI) during the degradation of peptides. The post-translational AAR and AAI could significantly induce the density and localization of plaque deposition in brain tissues. Alzheimer’s disease (AD) is reliably related to the formation and aggregation of amyloid-β peptide (Aβ) plaques in the human brain. No current analytical methods can simultaneously determine AAR and AAI during the degradation of Aβ from AD patients. We now report a covalent chiral derivatized ultraperformance liquid chromatography tandem mass spectrometry (CCD-UPLC-MS/MS) method for the determination of post-translational AAR and AAI of N-terminal Aβ (N-Aβ1–5) in human brain tissues. When subjected to tryptic N-Aβ1–5 from post-translationally modified natural Aβ in focal brain tissues by the CCD procedure, it was monitored at m/z 989.6→637.0/678.9 during electrospray collision-induced dissociation. These N-Aβ1–5 fragments with l-aspartic acid (l-Asp), d-Asp, l-isoAsp, and d-isoAsp could be separated using the UPLC system with a conventional reversed-phase column and mobile phase. The quantification of these peptides was determined using a stable isotope [15N]-labeled Aβ1–40 internal standard. The CCD-UPLC-MS/MS assay of potential N-Aβ1–5 allowed for the discovery of the present and ratio levels of these N-Aβ1–5 sequences with l-Asp, d-Asp, l-isoAsp, and d-isoAsp." @default.
• W2079462340 created "2016-06-24" @default.
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• W2079462340 date "2013-12-09" @default.
• W2079462340 modified "2023-10-09" @default.
• W2079462340 title "Simultaneous Determination of Post-Translational Racemization and Isomerization of <i>N</i>-Terminal Amyloid-β in Alzheimer’s Brain Tissues by Covalent Chiral Derivatized Ultraperformance Liquid Chromatography Tandem Mass Spectrometry" @default.
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• W2079462340 doi "https://doi.org/10.1021/ac403315h" @default.
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