The assembly of proteins and peptides in ordered fibrillar aggregates, namely amyloid fibrils, was recently related to many human neurodegenerative diseases. Amyloids oligomers are an intermediate step of this conversion process in which aggregation can lead, despite similar structural characteristics, to different toxic activity. Here we report on a Tip Enhanced Raman Spectroscopy study of HypF-N, a model protein forming amyloid oligomers, demonstrating how it is possible to distinguish their toxic and non-toxic forms by Raman analysis with nanometric resolution.
TIP ENHANCED RAMAN SPECTROSCOPY OF HYPF-N OLIGOMERS
2017
Abstract
The assembly of proteins and peptides in ordered fibrillar aggregates, namely amyloid fibrils, was recently related to many human neurodegenerative diseases. Amyloids oligomers are an intermediate step of this conversion process in which aggregation can lead, despite similar structural characteristics, to different toxic activity. Here we report on a Tip Enhanced Raman Spectroscopy study of HypF-N, a model protein forming amyloid oligomers, demonstrating how it is possible to distinguish their toxic and non-toxic forms by Raman analysis with nanometric resolution.File in questo prodotto:
Non ci sono file associati a questo prodotto.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
