Distinguishingd - andl -aspartic and isoaspartic acids in amyloid β peptides with ultrahigh resolution ion mobility spectrometry
| Autor: | Yehia M. Ibrahim, Richard D. Smith, Erin S. Baker, Vladislav A. Petyuk, Xueyun Zheng, Liulin Deng |
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| Rok vydání: | 2017 |
| Předmět: |
Protein Conformation
Ion-mobility spectrometry Stereoisomerism 010402 general chemistry Mass spectrometry 01 natural sciences Article Catalysis Protein structure Ion Mobility Spectrometry Materials Chemistry chemistry.chemical_classification Aspartic Acid Amyloid beta-Peptides Isoaspartic Acid Chemistry 010401 analytical chemistry Metals and Alloys General Chemistry Photo-reactive amino acid analog Peptide Fragments Amyloid β peptide 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Amino acid Ultrahigh resolution Biochemistry Ceramics and Composites |
| Zdroj: | Chemical Communications. 53:7913-7916 |
| ISSN: | 1364-548X 1359-7345 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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