Fourier transform infrared spectroscopy of amyloid proteins: In vitro and in situ studies.
Natalello A., Doglia S.M., Ami D.
Understanding the molecular mechanisms underlying protein and peptide aggregation is of great interest in different fields, ranging from new biomaterial development to human disease diagnosis and treatment. Among the different biophysical approaches, Fourier transform infrared (FTIR) spectroscopy has been shown to be a valuable tool to study the protein conformational changes that occur during amyloid fibril formation and to characterize the mature aggregates. Here, we applied FTIR (micro-)spectroscopy to study amyloid aggregation and co-aggregation $in vitro$ and $in situ$. The main outcomes of this label-free technique will be illustrated by amyloid-forming proteins involved in human diseases.