Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide 1-42.
The amyloid cascade hypothesis assigns the amyloid-beta peptide (Abeta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of Abeta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant Abeta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify Abeta(1-42), which is fully cytotoxic and able to form fibrils without any further refolding steps. The yield of the procedure is 5-8 mg of tag-less peptide per liter culture volume.
Wiesehan
Katja
K
Forschungszentrum Jülich, INB-2, 52425 Jülich, Germany.
Funke
Susanne Aileen
SA
Fries
Miriam
M
Willbold
Dieter
D
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000302:isolation & purification* / Q000494:pharmacology; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D017931:DNA Primers; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000494:pharmacology
D016229:Amyloid beta-Peptides; D017931:DNA Primers; D010446:Peptide Fragments; D011994:Recombinant Proteins; C075222:amyloid beta-protein (1-42)