ArticleBiophysical journal2011
Amyloid oligomer formation probed by water proton magnetic resonance spectroscopy.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy.Biophysical journal · 2019Article
- Article
- Hyperamylinemia contributes to cardiac dysfunction in obesity and diabetes: a study in humans and rats.Circulation research · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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Abstract
Formation of amyloid oligomers, the most toxic species of amyloids in degenerative diseases, is critically coupled to the interplay with surrounding water. The hydrophobic force driving the oligomerization causes water removal from interfaces, changing the surface-hydration properties. Here, we show that such effects alter the magnetic relaxation response of local water in ways that may enable oligomer detection. By using water proton magnetic resonance spectroscopy, we measured significantly longer transverse magnetic relaxation (T(2)) times in mixtures of serum and amyloidogenic Aβ(1-42) peptides versus similar concentration solutions of serum and nonamyloidogenic scrambled Aβ(42-1) peptides. Immunochemistry with oligomer-specific antibodies, electron microscopy and computer simulations demonstrated that the hyperintense magnetic signal correlates with Aβ(1-42) oligomerization. Finding early biophysical markers of the oligomerization process is crucial for guiding the development of new noninvasive imaging techniques, enabling timely diagnosis of amyloid-related diseases and pharmacological intervention.
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