Cesare M Baronio

Abstract Oligomers of the amyloid-beta peptide 1-42 (Abeta-42) are one of the underlying causes of pathogenicity in Alzheimer disease. However, investigating their molecular structure is challenging with common structural biology techniques. In this work we employed isotope-edited Fourier transform infrared spectroscopy with site-specific labeling, an advanced method enabling collection of residue-level structural information on oligomers of all sizes in aqueous solution.

Refining protein amide I spectrum simulations with simple yet effective electrostatic models for local wavenumbers and dipole derivative magnitudes† Analysis of the amide I band of proteins is probably the most wide-spread application of bioanalytical infrared spectroscopy. Although highly desirable for a more detailed structural interpretation, a quantitative description of this absorption band is still difficult.

Two main amyloid-? peptides of different length (A?40 and A?42) are involved in Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and mixed oligomers may contribute to the toxic species. However, little is know about the extent of mixing.