Fourier Transform Infrared Spectroscopy of Air-Dried and Heavy Water Suspended AA and AL Amyloid Fibril Preparations of Different Species
Amyloid deposits consist of amyloid fibrils and interfibrillar substance. On electron microscopy the fibrils of each type of amyloid and in different species are characterized as straight twisting fibrils of varying lengths and a diameter of about 10 nm. At high resolution, each fibril appears as two stranded ribbons. X-ray scattering of the dry fibrils of the various types reveals a cross ß pattern, while infrared spectroscopy reveals antiparallel ß-strands as a major structure. This led to the proposal of a model showing two twisting filaments of continuously stacked antiparallel ß-strands for all types of amyloid1. This model, however, does not incorporate non-ß conformations revealed by infrared spectroscopy of purified amyloid fibrils2, AA amyloid fibril fractions and reaggregated fibrils3. Recently these conformations were included in a model based on X-ray diffraction,of wet AA amyloid fibrils and secondary structure prediction of SAA4.
KeywordsAmyloid Deposit Amyloid Fibril Secondary Structure Prediction Heavy Water Major Structure
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