Abstract
Inhibition of β-amyloid (Aβ) aggregation in the cerebral cortex of the brain is a promising therapeutic and defensive strategy in identification of disease modifying agents for Alzheimer’s disease (AD). Since natural products are considered as the current alternative trend for the discovery of AD drugs, the present study aims at the evaluation of anti-amyloidogenic potential of the marine seaweed Padina gymnospora. Prevention of aggregation and disaggregation of the mature fibril formation of Aβ 25–35 by acetone extracts of P. gymnospora (ACTPG) was evaluated in two phases by Thioflavin T assay. The results were further confirmed by confocal laser scanning microscopy (CLSM) analysis and Fourier transform infrared (FTIR) spectroscopic analysis. The results of antiaggregation and disaggregation assay showed that the increase in fluorescence intensity of aggregated Aβ and the co-treatment of ACTPG (250 μg/ml) with Aβ 25–35, an extensive decrease in the fluorescence intensity was observed in both phases, which suggests that ACTPG prevents the oligomers formation and disaggregation of mature fibrils. In addition, ACTPG was subjected to column chromatography and the bioactivity was screened based on the cholinesterase inhibitory activity. Finally, the active fraction was subjected to LC-MS/MS analysis for the identification of bioactive compounds. Overall, the results suggest that the bioactive compound alpha bisabolol present in the alga might be responsible for the observed cholinesterase inhibition with the IC50 value < 10 μg/ml for both AChE and BuChE when compared to standard drug donepezil (IC50 value < 6 μg/ml) and support its use for the treatment of neurological disorders.
Highlights
Alzheimer’s disease (AD), an age related devastating neurodegenerative disorder results in cognitive impairments such as decision-making, language and behavioral activities
The present study was carried out to assess the inhibition of fibril formation by acetone extract of P. gymnospora (ACTPG) under in vitro conditions using Thioflavin T assay and the results were further validated through confocal microscopy study and Fourier Transform Infrared (FTIR) spectroscopic analysis
Antiaggregation and ChE Inhibitory Potential of P. gymnospora confirm that ACTPG exhibits anti-amyloidogenic effects
Summary
Alzheimer’s disease (AD), an age related devastating neurodegenerative disorder results in cognitive impairments such as decision-making, language and behavioral activities. Extracellular aggregates of Aβ was observed in AD patients, the most predominant one is Aβ 1–40 or Aβ 1–42; they contain peptides with shorter sequences such as Aβ 25–35 fragment containing a stretch of 11 full length amino acid residues. It forms itself β-sheet structure and produces similar effects to those produced by its parent sequence and has been found to be biologically active conferring toxicity to neurons [6]. It is related to the level of cognitive impairment in AD and local distribution of amyloid burden is often correlated with changes in the cognitive functions [9, 10]
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