Separation of amyloid β fragment peptides with racemised and isomerised aspartic acid residues using an original chiral resolution labeling reagent

Separation of amyloid β fragment peptides with racemised and isomerised aspartic acid residues using an original chiral resolution labeling reagent
复制标题

使用原始手性拆分标记试剂分离具有外消旋和异构化天冬氨酸残基的淀粉样蛋白 β 片段肽

DOI:
10.1039/d2an01885c
复制
发表时间:
2023
期刊:
The Analyst
影响因子:
--
通讯作者:
Hirose Tsunehisa
Hirose Tsunehisa
中科院分区:
--
文献类型:
--
作者:
Ozaki Makoto;Shimotsuma Motoshi;Kuranaga Takefumi;Kakeya Hideaki;Hirose Tsunehisa

文献摘要

相似文献

我们开发了一种分离和鉴定淀粉样蛋白β(Aβ)中消旋和异构化天冬氨酸(Asp)残基的方法,该方法采用了一种新颖的手性拆分标记试剂1-氟-2,4-二硝基苯-5-D-亮氨酸-N,N-二甲基乙二胺-酰胺(D-FDLDA)。用胰蛋白酶和内切蛋白酶Glu-C消化Aβ片段,在简单梯度条件下,用液相色谱-质谱法(LC-MS)分离和鉴定了D-FDLDA标记的外消旋和异构化天冬氨酸残基。此外,标记的Aβ片段不会聚集,并且在4 °C下至少保持稳定1周。
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.