Article
Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity.
ACS chemical biology - 17 Oct 2014
Mannini Benedetta, Mulvihill Estefania, Sgromo Caterina, Cascella Roberta, Khodarahmi Reza, Ramazzotti Matteo, Dobson Christopher M, Cecchi Cristina, Chiti Fabrizio
Abstract excerpt
The misfolding and aberrant assembly of peptides and proteins into fibrillar aggregates is the hallmark of many pathologies. Fibril formation is accompanied by oligomeric species thought to be the primary pathogenic agents in many of these diseases. With the aim of identifying the structural determinants responsible for the toxicity of misfolded oligomers, we created 12 oligomeric variants from the N-terminal...
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