Protein aggregation and toxicity in alzheimer's and parkinson disease Review

Roberto Dominici, Dario Finazzi, Chiara Paola Zoia, Giovanna M. Frasca, Lucio Tremolizzo, Ida Biunno

Research output: Contribution to journalArticlepeer-review

Abstract

Protein misfolding and aggregation into insoluble amyloid deposits are often associated with neurodegenerative disorders. The molecular mechanisms of aggregation from the native protein into amyloids involve several steps including protein misfolding, aggregation into oligomers, which seems to be the most toxic species, and, finally rearrangements into mature fibrils. In the present contribution, we review studies, illustrating various experimental approaches to dissect beta amyloid protein or α-synuclein behaviour in the context of Alzheimer and Parkinson's disease respectively, as well as of the details of the complicate aggregation mechanisms in which aberrant form of beta amyloid are involved. These aspects are of crucial relevance for a complete understanding of the onset of the protein conformational diseases and can also shed light on putative therapeutic targets and future development of aggregation inhibitors.

Original languageEnglish
Pages (from-to)285-300
Number of pages16
JournalAlzheimer's Disease Research Journal
Volume4
Issue number3
Publication statusPublished - 2011

Keywords

  • Amyloid-beta (Aβ) toxicity
  • Protein conformational neurodisorders
  • Protein misfolding and aggregation

ASJC Scopus subject areas

  • Clinical Neurology
  • Cellular and Molecular Neuroscience
  • Cognitive Neuroscience

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