Protein Conformational Misfolding and Amyloid Formation: Characteristics of a New Class of Disorders that Include Alzheimers and Prion Diseases

Title: Protein Conformational Misfolding and Amyloid Formation: Characteristics of a New Class of Disorders that Include Alzheimers and Prion Diseases

Volume: 9 Issue: 19

Author(s): Andrew J. Thompson and Colin J. Barrow

Affiliation:

Keywords: Amyloid Formation, Prion Diseases, Fibrillogenesis, Oxidative Stress

Abstract: The accumulation of proteinaceous deposits has been recognised to occur in several neurodegenerative conditions including Prion diseases, Alzheimers disease, Parkinsons disease, and Huntingtons disease. Over the last two decades interest in these conditions has increased markedly, fuelled partially by an increasing prevalence of these diseases in the Western world. Evidence indicates that anomalous protein misfolding and aggregation, with an accompanying “toxic gain of function” is central to the neuropathogenesis of these diseases. An increased understanding of the similarities and differences in the production, aggregation and accumulation of the respective proteins involved in these diseases, and the associated mechanisms of neurodegeneration, should aid in the development of new therapeutic agents to treat this group of related disorders.

Cite this article as:

Thompson J. Andrew and Barrow J. Colin, Protein Conformational Misfolding and Amyloid Formation: Characteristics of a New Class of Disorders that Include Alzheimers and Prion Diseases, Current Medicinal Chemistry 2002; 9 (19) . https://dx.doi.org/10.2174/0929867023369123