ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

• Structural features of amyloid fibrils highlighted by ATR-FTIR spectroscopy: a brief survey
• Conformational changes promoting fibrils formation
• Antiparallel β-sheet is the spectral feature of oligomers.
• Is the antiparallel β-sheet structure a signature of amyloid cytotoxicity?
• Organization of β-strands and β-sheet formation during aggregation

Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but are also implicated in important physiological functions (functional amyloids). The widespread presence of protein aggregates but also, in most of the cases, their deleterious effects explain worldwide efforts made to understand their formation, structure and biological functions. We emphasized the role of FTIR and especially ATR-FTIR techniques in amyloid protein and/or peptide studies. The multiple advantages provided by ATR-FTIR allow an almost continuous structural view of protein/peptide conversion during the aggregation process. Moreover, it is now well-established that infrared can differentiate oligomers from fibrils simply on their spectral features. ATR-FTIR is certainly the fastest and easiest method to obtain this information. ATR-FTIR occupies a key position in the analysis and comprehension of the complex aggregation mechanism(s) at the oligomer and/or fibril level. These mechanism(s) seem to present strong similarities between different amyloid proteins and might therefore be extremely important to understand for both disease-associated and functional amyloid proteins. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.

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