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. © Nova Science Publishers, Inc.
PROTEIN AGGREGATION AND TOXICITY IN ALZHEIMER'S AND PARKINSON DISEASE REVIEW
FINAZZI, Dario;
2011-01-01
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. © Nova Science Publishers, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
