Amyloid Oligomer Formation Probed by Water Proton Magnetic Resonance Spectroscopy

• Published in: Biophysical journal Vol. 100; no. 9; pp. 2302 - 2308
• Main Authors: Walton, J.H., Berry, R.S., Despa, F.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04.05.2011; Biophysical Society; The Biophysical Society
• Subjects: amyloid; Amyloid - chemistry; Amyloid - ultrastructure; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - ultrastructure; antibodies; Austenitic stainless steels; Biophysics; blood serum; computer simulation; Diseases; Electron microscopes; electron microscopy; Hydrophobic surfaces; hydrophobicity; image analysis; immunochemistry; Immunohistochemistry; Magnetic relaxation; Magnetic Resonance Spectroscopy; nuclear magnetic resonance spectroscopy; Oligomers; Peptides; Pharmacology; Protein; Protein Structure, Quaternary; Proton magnetic resonance; Protons; Serums; Spectroscopy; Spectrum analysis; Surface Properties; Time Factors; toxicity; Water; Water - chemistry

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...