Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Marcos J. Guerrero-Muñoz; Diana L. Castillo-Carranza; Rakez Kayed

doi:10.1016/j.bcp.2013.12.023

Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Marcos J. Guerrero-Muñoz, Diana L. Castillo-Carranza, Rakez Kayed

Neurology

Research output: Contribution to journal › Review article › peer-review

82 Scopus citations

Abstract

Impaired proteostasis is one of the main features of all amyloid diseases, which are associated with the formation of insoluble aggregates from amyloidogenic proteins. The aggregation process can be caused by overproduction or poor clearance of these proteins. However, numerous reports suggest that amyloid oligomers are the most toxic species, rather than insoluble fibrillar material, in Alzheimer's, Parkinson's, and Prion diseases, among others. Although the exact protein that aggregates varies between amyloid disorders, they all share common structural features that can be used as therapeutic targets. In this review, we focus on therapeutic approaches against shared features of toxic oligomeric structures and future directions.

Original language	English (US)
Pages (from-to)	468-478
Number of pages	11
Journal	Biochemical Pharmacology
Volume	88
Issue number	4
DOIs	https://doi.org/10.1016/j.bcp.2013.12.023
State	Published - Apr 15 2014

Keywords

Amyloid oligomers
Anti-amyloid small molecules
Immunotherapy

ASJC Scopus subject areas

Biochemistry
Pharmacology

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10.1016/j.bcp.2013.12.023

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abstract = "Impaired proteostasis is one of the main features of all amyloid diseases, which are associated with the formation of insoluble aggregates from amyloidogenic proteins. The aggregation process can be caused by overproduction or poor clearance of these proteins. However, numerous reports suggest that amyloid oligomers are the most toxic species, rather than insoluble fibrillar material, in Alzheimer's, Parkinson's, and Prion diseases, among others. Although the exact protein that aggregates varies between amyloid disorders, they all share common structural features that can be used as therapeutic targets. In this review, we focus on therapeutic approaches against shared features of toxic oligomeric structures and future directions.",

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AB - Impaired proteostasis is one of the main features of all amyloid diseases, which are associated with the formation of insoluble aggregates from amyloidogenic proteins. The aggregation process can be caused by overproduction or poor clearance of these proteins. However, numerous reports suggest that amyloid oligomers are the most toxic species, rather than insoluble fibrillar material, in Alzheimer's, Parkinson's, and Prion diseases, among others. Although the exact protein that aggregates varies between amyloid disorders, they all share common structural features that can be used as therapeutic targets. In this review, we focus on therapeutic approaches against shared features of toxic oligomeric structures and future directions.

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Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Abstract

Keywords

ASJC Scopus subject areas

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