XRD1 Highlights

UV Resonance Raman spectroscopy disentangled signals to unravel self-assembly modes of amyloid peptides in water

Detailed investigation using several techniques, including synchrotron-based UV Resonance Raman (UVRR) spectroscopy, sheds light on key differences in the Phe hydrophobic environment. E. Scarel et al., Soft Matter 18, 2129 (2022)

There is an increasing number of pathologies that are being linked to amyloid aggregates, such as Alzheimer’s and Parkinson’s diseases and cardiac amyloidoses and, recently, even therapeutic proteins have been found to form amyloids that can lead to local inflammation events (e.g., insulin). However, many details are still unknown pertaining the exact processes and modes of amyloid formation, and their physiological and pathological consequences.  A recent work that involved both the IUVS and XRD1 beamlines at Elettra allowed to unravel with atomistic detail how substitution of one L-Phe with its mirror-image D-Phe

to yield D-Phe-L- Phe maintains the ability of the peptide to form nanotubes, but suppresses their tendency to bundle into toxic microtubes. Retrieve Article Single-atom substitution enables supramolecular diversity from dipeptide building blocks Scarel E., Bellotto O., Rozhin P., Kralj S., Tortora M., Vargiu A. V., De Zorzi R., Rossi B.,  Marchesan S. Soft Matter 18, 2129 (2022) DOI: 10.1039/D1SM01824H