SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS
| Autor: | Modesto Orozco, Annalisa Arcella, Roberta Mazzucato, Marta Vilaseca, Natàlia Carulla, Rosa Pujol-Pina, Sílvia Vilaprinyó-Pascual |
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| Přispěvatelé: | Pujol-Pina R., Vilaprinyo-Pascual S., Mazzucato R., Arcella A., Vilaseca M., Orozco M., Carulla N. |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Spectrometry Mass Electrospray Ionization Amyloid beta-Peptide Biomedical Research Electrospray ionization Reproducibility of Result Peptide Mass spectrometry Oligomer Article chemistry.chemical_compound Peptide Fragment Alzheimer Disease Humans Sodium dodecyl sulfate Polyacrylamide gel electrophoresis chemistry.chemical_classification Amyloid beta-Peptides Multidisciplinary Aβ oligomers Reproducibility of Results Combinatorial chemistry Peptide Fragments Electrophoresis chemistry Thermodynamics Electrophoresis Polyacrylamide Gel Protein Multimerization Human |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep14809 |
| Popis: | The characterization of amyloid-beta peptide (Aβ) oligomer forms and structures is crucial to the advancement in the field of Alzheimer´s disease (AD). Here we report a critical evaluation of two methods used for this purpose, namely sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), extensively used in the field and ion mobility coupled to electrospray ionization mass spectrometry (ESI-IM-MS), an emerging technique with great potential for oligomer characterization. To evaluate their performance, we first obtained pure cross-linked Aβ40 and Aβ42 oligomers of well-defined order. Analysis of these samples by SDS-PAGE revealed that SDS affects the oligomerization state of Aβ42 oligomers, thus providing flawed information on their order and distribution. In contrast, ESI-IM-MS provided accurate information, while also reported on the chemical nature and on the structure of the oligomers. Our findings have important implications as they challenge scientific paradigms in the AD field built upon SDS-PAGE characterization of Aβ oligomer samples. |
| Databáze: | OpenAIRE |
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