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Degraded Products of Stem Bromelain Destabilize Aggregates of β-Amyloid Peptides Involved in Alzheimer’s Disease


Affiliations
1 Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India
 

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.
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  • Degraded Products of Stem Bromelain Destabilize Aggregates of β-Amyloid Peptides Involved in Alzheimer’s Disease

Abstract Views: 207  |  PDF Views: 64

Authors

Debratna Mukherjee
Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India
Payel Bhattacharjee
Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India
Reema Bhattacharya
Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India
Alok K. Dutta
Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India
Debasish Bhattacharyya
Division of Structural Biology and Bioinformatics, CSIR-Indian Institute of Chemical Biology 4, Raja S.C. Mallick Road, Jadavpur, Kolkata 700 032, India

Abstract


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.

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DOI: https://doi.org/10.18520/cs%2Fv115%2Fi11%2F2133-2141