Unraveling the Speciation of β-Amyloid Peptides during the Aggregation Process by Taylor Dispersion Analysis
| Autor: | Jean-François Hernandez, Joseph Chamieh, Luca Cipelletti, Mihai Deleanu, Jean-Philippe Biron, Myriam Taverna, Hervé Cottet, Emilie Rossi |
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| Přispěvatelé: | Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Charles Coulomb (L2C), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut Universitaire de France (IUF), Ministère de l'Education nationale, de l’Enseignement supérieur et de la Recherche (M.E.N.E.S.R.), Institut Galien Paris-Saclay (IGPS), Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2021 |
| Předmět: |
Taylor dispersion analysis
Hydrodynamic radius Taylor dispersion Peptide 010402 general chemistry 01 natural sciences Analytical Chemistry chemistry.chemical_compound β amyloid hydrodynamic radius Genetic algorithm amyloid beta peptides diffusion coefficient oligomers chemistry.chemical_classification Amyloid beta-Peptides 010401 analytical chemistry Peptide Fragments 0104 chemical sciences [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics Monomer chemistry Metals Ionic strength Scientific method Biophysics peptide aggregation [PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft] |
| Zdroj: | Analytical Chemistry Analytical Chemistry, American Chemical Society, 2021, 93 (16), pp.6523-6533. ⟨10.1021/acs.analchem.1c00527⟩ |
| ISSN: | 1520-6882 0003-2700 |
| DOI: | 10.1021/acs.analchem.1c00527 |
| Popis: | International audience; Aggregation mechanisms of amyloid β peptides depend on multiple intrinsic and extrinsic physicochemical factors (e.g., peptide chain length, truncation, peptide concentration, pH, ionic strength, temperature, metal concentration, etc.). Due to this high number of parameters, the formation of oligomers and their propensity to aggregate make the elucidation of this physiopathological mechanism a challenging task. From the analytical point of view, up to our knowledge, few techniques are able to quantify, in real time, the proportion and the size of the different soluble species during the aggregation process. This work aims at demonstrating the efficacy of the modern Taylor dispersion analysis (TDA) performed in capillaries (50 μm i.d.) to unravel the speciation of β-amyloid peptides in low-volume peptide samples (∼100 μL) with an analysis time of ∼3 min per run. TDA was applied to study the aggregation process of Aβ(1-40) and Aβ(1-42) peptides at physiological pH and temperature, where more than 140 data points were generated with a total volume of ∼1 μL over the whole aggregation study (about 0.5 μg of peptides). TDA was able to give a complete and quantitative picture of the Aβ speciation during the aggregation process, including the sizing of the oligomers and protofibrils, the consumption of the monomer, and the quantification of different early- and late-formed aggregated species. |
| Databáze: | OpenAIRE |
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