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ANS binding reveals common features of cytotoxic amyloid species

Journal Article


Abstract


  • 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 A beta(1-42) 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 A beta(1-42), the 159T 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.

Authors


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

Publication Date


  • 2010

Citation


  • Bolognesi, B., Kumita, J. R., Barros, T. P., Esbjorner, E. K., Luheshi, L., Crowther, D. C., Wilson, M. R., Dobson, C. M., Favrin, G. & Yerbury, J. (2010). ANS binding reveals common features of cytotoxic amyloid species. ACS Chemical Biology, 5 (8), 735-740.

Scopus Eid


  • 2-s2.0-77955881152

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/974

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 735

End Page


  • 740

Volume


  • 5

Issue


  • 8

Abstract


  • 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 A beta(1-42) 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 A beta(1-42), the 159T 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.

Authors


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

Publication Date


  • 2010

Citation


  • Bolognesi, B., Kumita, J. R., Barros, T. P., Esbjorner, E. K., Luheshi, L., Crowther, D. C., Wilson, M. R., Dobson, C. M., Favrin, G. & Yerbury, J. (2010). ANS binding reveals common features of cytotoxic amyloid species. ACS Chemical Biology, 5 (8), 735-740.

Scopus Eid


  • 2-s2.0-77955881152

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/974

Has Global Citation Frequency


Number Of Pages


  • 5

Start Page


  • 735

End Page


  • 740

Volume


  • 5

Issue


  • 8