Aggregation of amyloid A beta((1-40)) peptide in perdeuterated 2,2,2-trifluoroethanol caused by ultrasound sonication
Filippov, Andrei V., Grobner, Gerhard and Antzutkin, Oleg N.. (2010) Aggregation of amyloid A beta((1-40)) peptide in perdeuterated 2,2,2-trifluoroethanol caused by ultrasound sonication. Magnetic Resonance in Chemistry, Vol.48 (No.6). pp. 427-434. ISSN 0749-1581Full text not available from this repository.
Official URL: http://dx.doi.org/10.1002/mrc.2596
Ultrasound sonication of protein and peptide solutions is routinely used in biochemical, biophysical, pharmaceutical and medical sciences to facilitate and accelerate dissolution of macromolecules in both aqueous and organic solvents. However, the impact of ultrasound waves on folding/unfolding of treated proteins, in particular, on aggregation kinetics of amyloidogenic peptides and proteins is not understood. In this work, effects of ultrasound sonication on the misfolding and aggregation behavior of the Alzheimer's A beta((1-40))-peptide is studied by pulsed-field gradient (PFG) spin-echo diffusion NMR and UV circular dichroism (CD) spectroscopy. Upon simple dissolution of A beta((1-40)) in perdeuterated trifluoroethanol, CF3-CD2-OD (TFE-d(3)), the peptide is present in the solution as a stable monomer adopting alpha-helical secondary structural motifs. The self-diffusion coefficient of A beta((1-40)) monomers in TFE-d(3) was measured as 1.35 x 10(-10) m(2) s(-1), reflecting its monomeric character. However, upon ultrasonic sonication for less than 5 min, considerable populations of A beta molecules (ca 40%) form large aggregates as reflected in diffusion coefficients smaller than 4.0 x 10(-13) m(2) s(-1). Sonication for longer times (up to 40 min in total) effectively reduces the fraction of these aggregates in H-1 PFG NMR spectra to ca 25%. Additionally, absorption below 230 nm increased significantly upon sonication treatment, an observation, which also clearly confirms the ongoing aggregation process of A beta((1-40)) in TFE-d(3). Surprisingly, upon ultrasound sonication only small changes in the peptide secondary structure were detected by CD: the peptide molecules mainly adopt alpha-helical motifs in both monomers and aggregates formed upon sonication. Copyright (C) 2010 John Wiley & Sons, Ltd.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QC Physics
|Divisions:||Faculty of Science > Physics|
|Journal or Publication Title:||Magnetic Resonance in Chemistry|
|Publisher:||John Wiley & Sons Ltd.|
|Number of Pages:||8|
|Page Range:||pp. 427-434|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Kempe Foundations, Swedish Research Council|
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