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Bhattacharjee, Payel
- Degraded Products of Stem Bromelain Destabilize Aggregates of β-Amyloid Peptides Involved in Alzheimer’s Disease
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PDF Views:67
Authors
Debratna Mukherjee
1,
Payel Bhattacharjee
1,
Reema Bhattacharya
1,
Alok K. Dutta
1,
Debasish Bhattacharyya
1
Affiliations
1 Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, IN
1 Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, IN
Source
Current Science, Vol 115, No 11 (2018), Pagination: 2133-2141Abstract
Deposition of fibrils originating from monomeric β- amyloid (Aβ) peptide in brain cells is responsible for progressive neuronal damages in Alzheimer’s disease. Peptides from bromelain, a cysteine protease from Ananas comosus (pineapple), were generated after digestion with proteases under conditions similar to human gastrointestinal tract. These peptides not only inhibit the growth of Aβ-amyloid aggregates, but also irreversibly destabilize the preformed aggregates. Gel filtration followed by mass spectrometric analysis identified a pool of peptides of <700 Da in the digest. Probable composition of the peptides interacting with Aβ-peptide was predicted from homology alignment between Aβ-peptide and bromelain using bioinformatics tools. Corresponding synthetic peptides can also destabilize the preformed aggregates as observed from thioflavin T assay, transmission electron microscopy and atomic force microscopy. Aβ aggregates that were preincubated with the bromelain-derived peptides did not exert appreciable toxicity on human neuroblastoma cells (SH-SY5Y) cultured in vitro.Keywords
Alzheimer’s Disease, Aβ Peptide, Disaggregation, Stem Bromelain.Full Text
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