Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins |
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Affiliation: | 1. Department of Orthopaedics, Tangdu Hospital, The Fourth Military Medical University, Xi''an 710032, China;2. Department of Neurology, Xijing Hospital, The Fourth Military Medical University, Xi''an 710032, China;3. Department of Clinical Aerospace Medicine, The Fourth Military Medical University, Xi''an 710032, China;4. Diagnosis, Treatment and Rehabilitation Center of Neurological Diseases, Second Sanatorium, Qingdao 266071, China;5. Department of Health Service, Faculty of Aerospace, The Fourth Military Medical University, Xi''an 710032, China |
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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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Keywords: | Amyloid oligomers Immunotherapy Anti-amyloid small molecules Methylene blue (PubChem CID: 6099) Epigallocatechingallate (PubChem CID: 65064) Curcumin (PubChem CID: 969516) Resveratrol (PubChem CID: 445154) Oleuropein (PubChem CID: 5281544) Baicalein (PubChem CID: 5281605) Phenol Red (PubChem CID: 4766) Silibinin (PubChem CID: 31553) CLR01 (http://www.med-chemist.com/2012/11/clr01-effectively-inhibits.html) |
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