Abstract
Background:
Alzheimer's disease (AD) is diagnosed with the deposition of insoluble β-amyloid (Aβ) peptides in the neuropil of the brain leading to dementia. The extracellular deposition of the fibrillar Aβ peptide on the neurons is known as senile plaques. Therefore, Aβ degradation and clearance from the human body is a promising therapeutic approach in the medication of AD.
Methods:
In the current study, the enzyme lumbrokinase (LK) was extracted and purified from earthworm and its activity was utilized toward Aβ 1-42 amyloids degradation in vitro alongside with an additional enzyme serratiopeptidase (SP) considering nattokinase (NK) as a standard.
Results:
The output of this study revealed that preformed Aβ 1-42 amyloids was disintegrated by both LK and SP, as demonstrated from fluorescence assay using Thioflavin T dye. In addition, dynamic light scattering study revealed the lower size of the preformed fibrils Aβ 1-42 at various time intervals after incubation with the enzymes LK and SP. Furthermore, in silico approach showed high affinity thermodynamically favorable interaction of LK as well as SP toward Aβ 1-42 amyloid. Finally, the toxicity of degraded preformed Aβ 1-42 amyloid was assessed by MTT assay which showed reduced toxicity of enzyme treated Aβ 1-42 amyloid compared to only Aβ 1-42 amyloid.
Conclusion:
The findings of the present study indicated that LK and SP, not only had Aβ 1-42 amyloid degrading potential, but also could reduce the toxicity which can make them a suitable drug candidate for AD. Furthermore, the in vivo studies are needed to be executed in future.
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