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

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

Neuroprotective Strategies for Neurological Disorders by Natural Products: An update

“…The Aβ also reported to be accumulated within the neurons which lead to synaptic dysfunction, cognitive impairment and Aβ plaques formation [98]. Various effective therapeutic molecules have been reported to suppress the formation of Aβ plaques for the treatment of Alzheimer’s disease [99, 100]. Keeping in view the cost of treatment for Alzheimer’s disease and the limitations associated with the previous preventive techniques, natural products including nutraceuticals have gained paramount importance [5].…”

Exploring the Transition of Human α-Synuclein from Native to the Fibrillar State: Insights into the Pathogenesis of Parkinson’s Disease

“…8a, fluorescence spectra of ThT dye almost touches the baseline (curve 1) and the fluorescence intensity of 100 μM pendimethalin again represents a weak spectra very near to that of the ThT dye (curve 2). Native state of protein displays a low level of spectra (curve 3) as opposed to the 10 and 12 h incubated samples in which there is almost 9 and 10 fold increase in fluorescence intensity with λ max at around 496 nm (curves 4,5). This hike in the fluorescence intensity suggests that the ThT conformers would have stuck to the β-sheets present in the fibrillar structure via electrostatic and hydrophobic interactions.…”

“…These include Alzheimer's, Parkinson's and Huntington's disease, type II diabetes, spongiform encephalopathy, primary and secondary systemic amyloidosis [4][5][6]. Of specific interest is Parkinson's disease which involves the fibrillation of a natively unstructured protein [7].…”

Nanomaterials in Alzheimer’s disease treatment: a comprehensive review

“…AD adversely progresses with age as the major risk factor, the disease doubles exponentially every five years after the age of 65 [2][3][4]. The persistent lacuna remains in the diagnosis of AD that fails to establish a full-proof diagnosis except for post-mortem identification of AD characteristics such as NFTs and SPs [5,6]. Premortem reports of the neurological, cognitive and neurophysiological tests as well as in vivo brain imaging in addition to patient's clinical history, have proven to provide maximal accuracy of 85% [5].…”

“…The persistent lacuna remains in the diagnosis of AD that fails to establish a full-proof diagnosis except for post-mortem identification of AD characteristics such as NFTs and SPs [5,6]. Premortem reports of the neurological, cognitive and neurophysiological tests as well as in vivo brain imaging in addition to patient's clinical history, have proven to provide maximal accuracy of 85% [5]. The trajectory of AD begins with healthy aging, preclinical AD that progresses to MCI and ultimately leads to dementia.…”