Amyloid oligomer formation probed by water proton magnetic resonance spectroscopy

J. H. Walton, R. S. Berry, F. Despa

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Formationofamyloid oligomers, the most toxic speciesofamyloidsindegenerative diseases,iscritically 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 (T2) times in mixtures of serum and amyloidogenic Aβ1-42 peptides versus similar concentration solutions ofserum and nonamyloidogenic scrambled Aβ42-1 peptides. Immunochemistry with oligomer-specific antibodies, electron microscopy and computer simulations demonstrated that the hyperintense magnetic signal correlates with Aβ1-42 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.

Original languageEnglish
Pages (from-to)2302-2308
Number of pages7
JournalBiophysical Journal
Issue number9
StatePublished - May 4 2011

Bibliographical note

Funding Information:
The work was supported by the American Heart Association under grant No. 09BGIA2220165 (to F.D.) and by the Vision Grant from UC Davis Health System (to F.D.).

ASJC Scopus subject areas

  • Biophysics


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