Literature DB >> 23820032

Inhibiting toxic aggregation of amyloidogenic proteins: a therapeutic strategy for protein misfolding diseases.

Biao Cheng1, Hao Gong, Hongwen Xiao, Robert B Petersen, Ling Zheng, Kun Huang.   

Abstract

BACKGROUND: The deposition of self-assembled amyloidogenic proteins is associated with multiple diseases, including Alzheimer's disease, Parkinson's disease and type 2 diabetes mellitus. The toxic misfolding and self-assembling of amyloidogenic proteins are believed to underlie protein misfolding diseases. Novel drug candidates targeting self-assembled amyloidogenic proteins represent a potential therapeutic approach for protein misfolding diseases. SCOPE OF REVIEW: In this perspective review, we provide an overview of the recent progress in identifying inhibitors that block the aggregation of amyloidogenic proteins and the clinical applications thereof. MAJOR
CONCLUSIONS: Compounds such as polyphenols, certain short peptides, and monomer- or oligomer-specific antibodies, can interfere with the self-assembly of amyloidogenic proteins, prevent the formation of oligomers, amyloid fibrils and the consequent cytotoxicity. GENERAL SIGNIFICANCE: Some inhibitors have been tested in clinical trials for treating protein misfolding diseases. Inhibitors that target the aggregation of amyloidogenic proteins bring new hope to therapy for protein misfolding diseases.
© 2013.

Entities:  

Keywords:  (−)-epigallocatechin 3-gallate; AChE; AD; AIF; Alzheimer's disease; Amyloid; Aβ; BBB; C/EBP Homologous Protein; CA; CD; CGA; CHOP; CNS; Cytotoxicity; EGCG; ER; FAP; HD; Htt; Huntington disease; Inhibitor; PD; PICUP; PMDs; Parkinson's disease; Polyphenols; Protein misfolding disease; ROS; SAR; T2DM; acetylcholinesterase; amyloid-beta; apoptosis induce factor; blood brain barrier; caffeic acid; central nervous system; chlorogenic acid; circular dichroism; endoplasmic reticulum; familial amyloid polyneuropathy; huntingtin; photo-induced cross-linking of unmodified proteins; protein misfolding diseases; reactive oxygen species; structure–activity relationships; type 2 diabetes mellitus

Mesh:

Substances:

Year:  2013        PMID: 23820032     DOI: 10.1016/j.bbagen.2013.06.029

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  45 in total

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4.  Epigallocatechin-3-gallate Inhibits Cu(II)-Induced β-2-Microglobulin Amyloid Formation by Binding to the Edge of Its β-Sheets.

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Review 7.  Invasive and non-invasive therapies for Alzheimer's disease and other amyloidosis.

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Review 8.  Use of genetically modified mesenchymal stem cells to treat neurodegenerative diseases.

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Review 9.  Oleuropein aglycone and polyphenols from olive mill waste water ameliorate cognitive deficits and neuropathology.

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10.  Epigallocatechin Gallate (EGCG) Inhibits Alpha-Synuclein Aggregation: A Potential Agent for Parkinson's Disease.

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Journal:  Neurochem Res       Date:  2016-06-30       Impact factor: 3.996

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