Details

Autor(en) / Beteiligte

• Bolognesi, Benedetta
• Kumita, Janet R.
• Barros, Teresa P.
• Esbjorner, Elin K.
• Luheshi, Leila M.
• Crowther, Damian C.
• Wilson, Mark R.
• Dobson, Christopher M.
• Favrin, Giorgio
• Yerbury, Justin J.

Titel

ANS Binding Reveals Common Features of Cytotoxic Amyloid Species

Ist Teil von

• ACS chemical biology, 2010-08, Vol.5 (8), p.735-740

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2010

Quelle

MEDLINE

Beschreibungen/Notizen

• Oligomeric assemblies formed from a variety of disease-associated peptides and proteins have been strongly associated with toxicity in many neurodegenerative conditions, such as Alzheimer’s disease. The precise nature of the toxic agents, however, remains still to be established. We show that prefibrillar aggregates of E22G (arctic) variant of the Aβ1−42 peptide bind strongly to 1-anilinonaphthalene 8-sulfonate and that changes in this property correlate significantly with changes in its cytotoxicity. Moreover, we show that this phenomenon is common to other amyloid systems, such as wild-type Aβ1–42, the I59T variant of human lysozyme and an SH3 domain. These findings are consistent with a model in which the exposure of hydrophobic surfaces as a result of the aggregation of misfolded species is a crucial and common feature of these pathogenic species.