Change search
ReferencesLink to record
Permanent link

Direct link
Aggregation of amyloid Aβ(1-40) peptide in perdeuterated 2,2,2-trifluoroethanol caused by ultrasound sonication
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2010 (English)In: Magnetic Resonance in Chemistry, ISSN 0749-1581, E-ISSN 1097-458X, Vol. 48, no 6, 427-34 p.Article in journal (Refereed) Published
Abstract [en]

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 Aβ(1-40)-peptide is studied by pulsed-field gradient (PFG) spin-echo diffusion NMR and UV circular dichroism (CD) spectroscopy. Upon simple dissolution of Aβ(1-40) in perdeuterated trifluoroethanol, CF3-CD2-OD (TFE-d3), the peptide is present in the solution as a stable monomer adopting -helical secondary structural motifs. The self-diffusion coefficient of Aβ(1-40) monomers in TFE-d3 was measured as 1.35 × 10-10 m2 s-1, reflecting its monomeric character. However, upon ultrasonic sonication for less than 5 min, considerable populations of A molecules (ca 40%) form large aggregates as reflected in diffusion coefficients smaller than 4.0 × 10-13 m2 s-1. Sonication for longer times (up to 40 min in total) effectively reduces the fraction of these aggregates in 1H 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 Aβ(1-40) in TFE-d3. Surprisingly, upon ultrasound sonication only small changes in the peptide secondary structure were detected by CD: the peptide molecules mainly adopt -helical motifs in both monomers and aggregates formed upon sonication.

Place, publisher, year, edition, pages
John Wiley & Sons, Ltd. , 2010. Vol. 48, no 6, 427-34 p.
Keyword [en]
pulsed-field gradient 1H NMR, translational self-diffusion, Alzheimer's Aβ(1-40) peptide, deuterated trifluoroethanol, peptide aggregation, peptide secondary structure
URN: urn:nbn:se:umu:diva-33205DOI: 10.1002/mrc.2596ISI: 000278041200002OAI: diva2:310929
"E-pub before print"Available from: 2010-04-19 Created: 2010-04-19 Last updated: 2010-05-11Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Gröbner, Gerhard
By organisation
Department of Chemistry
In the same journal
Magnetic Resonance in Chemistry

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 104 hits
ReferencesLink to record
Permanent link

Direct link