Zheng Xueyun, Deng Liulin, Baker Erin S, Ibrahim Yehia M, Petyuk Vladislav A, Smith Richard D
Biological Sciences Division, Pacific Northwest National Laboratory, 902 Battelle Boulevard, Richland, WA 99352, USA.
Chem Commun (Camb). 2017 Jul 11;53(56):7913-7916. doi: 10.1039/c7cc03321d.
While α-linked amino acids in the l-form are exclusively utilized in mammalian protein building, β-linked and d-form amino acids also have important biological roles. Unfortunately, the structural elucidation and separation of these different amino acid types in peptides has been analytically challenging to date due to the numerous isomers present, limiting our knowledge about their existence and biological roles. Here, we utilized an ultrahigh resolution ion mobility spectrometry platform coupled with mass spectrometry (IMS-MS) to separate amyloid β (Aβ) peptides containing l-aspartic acid, d-aspartic acid, l-isoaspartic acid, and d-isoaspartic acid residues which span α- and β-linked amino acids in both d- and l-forms. The results illustrate how IMS-MS could be used to better understand age-related diseases or protein folding disorders resulting from amino acid modifications.
虽然L型α-连接氨基酸仅用于哺乳动物蛋白质的构建，但β-连接氨基酸和D型氨基酸也具有重要的生物学作用。不幸的是，由于存在众多异构体，迄今为止，肽中这些不同类型氨基酸的结构解析和分离在分析上具有挑战性，这限制了我们对它们的存在和生物学作用的了解。在这里，我们利用超高分辨率离子淌度光谱平台与质谱联用（IMS-MS）来分离含有L-天冬氨酸、D-天冬氨酸、L-异天冬氨酸和D-异天冬氨酸残基的淀粉样β（Aβ）肽，这些残基涵盖了D型和L型的α-连接和β-连接氨基酸。结果表明了IMS-MS如何可用于更好地理解由氨基酸修饰导致的与年龄相关的疾病或蛋白质折叠紊乱。
