A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.

A hydrophobic gold surface triggers misfolding and aggregation of the amyloidogenic Josephin domain in monomeric form, while leaving the oligomers unaffected.

Protein misfolding and aggregation in intracellular and extracellular spaces is regarded as a main marker of the presence of degenerative disorders such as amyloidoses. To elucidate the mechanisms of protein misfolding, the interaction of proteins with inorganic surfaces is of particular relevance,...

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Bibliographic Details
Main Authors: Alessandra Apicella, Monica Soncini, Marco Agostino Deriu, Antonino Natalello, Marcella Bonanomi, David Dellasega, Paolo Tortora, Maria Elena Regonesi, Carlo Spartaco Casari
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23527026/?tool=EBI

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https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23527026/?tool=EBI

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