Separation of amyloid β fragment peptides with racemised and isomerised aspartic acid residues using an original chiral resolution labeling reagent.
Makoto OzakiMotoshi ShimotsumaTakefumi KuranagaHideaki KakeyaTsunehisa HirosePublished in: The Analyst (2023)
We developed a system to separate and identify racemised and isomerised aspartic acid (Asp) residues in amyloid β (Aβ) by labeling with an original chiral resolution labeling reagent, 1-fluoro-2,4-dinitrophenyl-5-D-leucine- N , N -dimethylethylenediamine-amide (D-FDLDA). The racemised and isomerised Asp residues labeled with D-FDLDA in Aβ fragments generated by digesting with trypsin and endoproteinase Glu-C were separated and identified by liquid chromatography-mass spectrometry (LC-MS) under simple gradient conditions. Furthermore, the labeled Aβ fragments did not aggregate and remained stable at least for 1 week at 4 °C.
Keyphrases
- liquid chromatography
- mass spectrometry
- capillary electrophoresis
- high resolution mass spectrometry
- tandem mass spectrometry
- pet imaging
- simultaneous determination
- single molecule
- gas chromatography
- high performance liquid chromatography
- ionic liquid
- positron emission tomography
- high resolution
- solid phase extraction
- computed tomography
- study protocol
- pet ct