A peptide fraction of Olive Flounder (Paralichthys olivaceus) Skin Hydrolysate Inhibits Amyloid-β Generation in SH-SY5Y Cells via Suppression of BACE1 Expression

The prevalence of degenerative neuro-diseases such as Alzheimer's disease has increased with an increase in the life expectancy especially as seen in developed countries. According to the Amyloid Hypothesis, beta-secretase leads to the onset of Alzheimer's disease though the generation of amyloid-beta by proteolysis of amyloid precursor protein. Amyloid-beta aggregates to form oligomers that build up to form plaques. Olive flounder (Paralichthys olivaceus) is high in protein content, with a higher protein content in skin (27.65%) compared to muscle (19.65%) according to proximate analysis results. Enzyme hydrolysates were prepared from skin and muscle using several enzymes. The neutrase skin hydrolysate showed the highest beta-secretase inhibitory activity IC50 0.61 mg/mL. Purification steps were performed using ion exchange chromatography on QMA and CM-cellulose columns and SPE C18 column to produce an active fraction QMA-F1 with an IC50 value of 32.80 mu g/mL. QMA-F1 was non-cytotoxic to SH-SY5Y cells, reduced BACE1 overexpression and attenuated amyloidogenesis. This suggests that the active beta-secretase inhibitory peptides from olive flounder skin hydrolysates can be utilized as an ingredient in development of new pharmaceutical and nutraceutical therapeutic agents for Alzheimer's Disease.

Automated summary

The study found that peptides in the olive flounder skin hydrolysates can effectively inhibit beta-secretase activity, potentially serving as ingredients for new pharmaceutical and nutraceutical agents for the treatment of Alzheimer's Disease.