Therapeutic Interventions for the Suppression of Alzheimer's Disease: Quest for a Remedy

• Published in: Current drug metabolism Vol. 16; no. 5; p. 346
• Main Authors: Fazili, Naveed Ahmad, Naeem, Aabgeena, Ashraf, Ghulam Md, Hua, Gan Siew, Kamal, Mohammad A
• Format: Journal Article
• Language: English
• Published: Netherlands 01.06.2015
• Subjects: Alzheimer Disease - drug therapy; Alzheimer Disease - physiopathology; Amyloid - metabolism; Amyloid beta-Peptides - metabolism; Animals; Drug Design; Humans; Protein Aggregation, Pathological - prevention & control; Protein Folding; Protein Structure, Secondary
• ISSN: 1875-5453
• DOI: 10.2174/1389200215999141125115749

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 Aβ amyloids, and suggests a positive future for the eradication of this dreaded disease.