Abstract
Accumulating evidence suggests that Aβ1–42–membrane interactions may play an important role in the pathogenesis of Alzheimer’s disease. However, the mechanism of this structural transition remains unknown. In this work, we have shown that submicellar concentrations of sodium dodecyl sulfate (SDS) can provide a minimal platform for Aβ1–42 self-assembly. To further investigate the relation between Aβ1–42 structure and function, we analyzed peptide conformation and aggregation at various SDS concentrations using circular dichroism (CD), Fourier transform infrared spectroscopy, and gel electrophoresis. These aggregates, as observed via atomic force microscopy, appeared as globular particles in submicellar SDS with diameters of 35–60 nm. Upon sonication, these particles increased in disc diameter to 100 nm. Pyrene I 3/I 1 ratios and 1-anilinonaphthalene-8-sulfonic acid binding studies indicated that the peptide interior is more hydrophobic than the SDS micelle interior. We have also used Forster resonance energy transfer between N-terminal labeled pyrene and tyrosine (10) of Aβ1–42 in various SDS concentrations for conformational analysis. The results demonstrate that SDS at submicellar concentrations accelerates the formation of spherical aggregates, which act as niduses to form large spherical aggregates upon sonication.
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Abbreviations
- Aβ1–42 :
-
Amyloid β peptide, a 42 residue peptide
- AFM:
-
Atomic force microscopy
- ANS:
-
1-Anilinonapthalene-8-sulfonic acid ammonium salt
- CD:
-
Circular dichroism
- FRET:
-
Forster resonance energy transfer
- FTIR:
-
Fourier transformed infrared spectroscopy
- SDS:
-
Sodium dodecyl sulfate
- TFA:
-
Trifluoro acetic acid
- TFE:
-
2,2,2 Trifluoroethanol
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Acknowledgments
We thank Dr. T. Ramasami, Director, CLRI, for his kind support for this work. One of the author, N. Sureshbabu thanks the Council for Scientific and Industrial Research (CSIR) for providing funds in the form of SRF. We also thank Dr. Ganesh, Vanderbilt University, for his help with peptide synthesis.
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Sureshbabu, N., Kirubagaran, R. & Jayakumar, R. Surfactant-induced conformational transition of amyloid β-peptide. Eur Biophys J 38, 355–367 (2009). https://doi.org/10.1007/s00249-008-0379-8
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DOI: https://doi.org/10.1007/s00249-008-0379-8