A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease

Kerensa Broersen, Wim Jonckheere, Jef Rozenski, A. Vandersteen, Annelies Vandersteen, Kris Pauwels, Annalisa Pastore, Frederic Rousseau, Joost Schymkowitz

Research output: Contribution to journalArticleAcademicpeer-review

60 Citations (Scopus)

Abstract

We provide a validated and rapid protocol for the solubilization of amyloid β-peptide (Aβ). This procedure involves sequential solubilization using structure-breaking organic solvents hexafluoroisopropanol and DMSO followed by column purification. The low solubility and tendency of Aβ to aggregate considerably impede the in vitro handling and biophysical or biological investigation of Aβ, despite the interest in this peptide because of its implication in Alzheimer's disease. The main advantage of the proposed protocol over others is that it results in standardized aggregate-free Aβ peptide samples that are biocompatible for cell culture studies and yield reproducible aggregation kinetics and cytotoxicities. This three-step protocol also enables the co-solubilization of the longer Aβ42 variant with Aβ40 in ratios relevant to Alzheimer's disease.
Original languageUndefined
Pages (from-to)743-750
Number of pages8
JournalProtein engineering design & selection
Volume24
Issue number9
DOIs
Publication statusPublished - 2011

Keywords

  • METIS-279064
  • IR-104449

Cite this

Broersen, Kerensa ; Jonckheere, Wim ; Rozenski, Jef ; Vandersteen, A. ; Vandersteen, Annelies ; Pauwels, Kris ; Pastore, Annalisa ; Rousseau, Frederic ; Schymkowitz, Joost. / A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease. In: Protein engineering design & selection. 2011 ; Vol. 24, No. 9. pp. 743-750.
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Broersen, K, Jonckheere, W, Rozenski, J, Vandersteen, A, Vandersteen, A, Pauwels, K, Pastore, A, Rousseau, F & Schymkowitz, J 2011, 'A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease' Protein engineering design & selection, vol. 24, no. 9, pp. 743-750. https://doi.org/10.1093/protein/gzr020

A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease. / Broersen, Kerensa; Jonckheere, Wim; Rozenski, Jef; Vandersteen, A.; Vandersteen, Annelies; Pauwels, Kris; Pastore, Annalisa; Rousseau, Frederic; Schymkowitz, Joost.

In: Protein engineering design & selection, Vol. 24, No. 9, 2011, p. 743-750.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease

AU - Broersen, Kerensa

AU - Jonckheere, Wim

AU - Rozenski, Jef

AU - Vandersteen, A.

AU - Vandersteen, Annelies

AU - Pauwels, Kris

AU - Pastore, Annalisa

AU - Rousseau, Frederic

AU - Schymkowitz, Joost

PY - 2011

Y1 - 2011

N2 - We provide a validated and rapid protocol for the solubilization of amyloid β-peptide (Aβ). This procedure involves sequential solubilization using structure-breaking organic solvents hexafluoroisopropanol and DMSO followed by column purification. The low solubility and tendency of Aβ to aggregate considerably impede the in vitro handling and biophysical or biological investigation of Aβ, despite the interest in this peptide because of its implication in Alzheimer's disease. The main advantage of the proposed protocol over others is that it results in standardized aggregate-free Aβ peptide samples that are biocompatible for cell culture studies and yield reproducible aggregation kinetics and cytotoxicities. This three-step protocol also enables the co-solubilization of the longer Aβ42 variant with Aβ40 in ratios relevant to Alzheimer's disease.

AB - We provide a validated and rapid protocol for the solubilization of amyloid β-peptide (Aβ). This procedure involves sequential solubilization using structure-breaking organic solvents hexafluoroisopropanol and DMSO followed by column purification. The low solubility and tendency of Aβ to aggregate considerably impede the in vitro handling and biophysical or biological investigation of Aβ, despite the interest in this peptide because of its implication in Alzheimer's disease. The main advantage of the proposed protocol over others is that it results in standardized aggregate-free Aβ peptide samples that are biocompatible for cell culture studies and yield reproducible aggregation kinetics and cytotoxicities. This three-step protocol also enables the co-solubilization of the longer Aβ42 variant with Aβ40 in ratios relevant to Alzheimer's disease.

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KW - IR-104449

U2 - 10.1093/protein/gzr020

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M3 - Article

VL - 24

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EP - 750

JO - Protein engineering design & selection

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