Abstract
Protein aggregation is facilitated by the generation of partially folded intermediates that lack most of the tertiary interactions, but retain the complete secondary structure. These partially folded states cross-link each other to form protein aggregates. Protein aggregates in an advanced stage result in the formation of amyloid fibrils, which have high tensile strength. These amyloid fibrils are associated with a number of pathologies, especially Alzheimer's disease, which involves the aggregation of the Aβ peptide. In recent years, much attention has been paid to the generation of potent therapeutics to reduce Aβ peptide fibrillation. This review summarizes the range of molecules used for this therapy, showing their potency against Aβamyloids, and suggests a positive future for the eradication of this dreaded disease.
Original language | English |
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Pages (from-to) | 346-353 |
Number of pages | 8 |
Journal | Current Drug Metabolism |
Volume | 16 |
Issue number | 5 |
DOIs | |
Publication status | Published - 1 Jun 2015 |
Externally published | Yes |
Keywords
- Alzheimer's disease
- Amyloid fibrils
- Aβpeptide
- Nanotechnological approach
- Protein aggregates