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Gelatin grafted poly( D,L ‐ lactide ) as an inhibitor of protein aggregation: An in vitro case study
Author(s) -
Balavigneswaran Chelladurai Karthikeyan,
Kumar Gaurav,
Vignesh Kumar Chandrasekaran,
Sellamuthu Satheeshkumar,
Kasiviswanathan Uvanesh,
Ray Biswajit,
Muthuvijayan Vignesh,
Mahto Sanjeev Kumar,
Misra Nira
Publication year - 2020
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23383
Subject(s) - chemistry , gelatin , fibril , thioflavin , bovine serum albumin , circular dichroism , protein aggregation , in vitro , amyloid (mycology) , biophysics , biochemistry , alzheimer's disease , medicine , inorganic chemistry , disease , pathology , biology
Amyloids are a group of proteins that are capable of forming aggregated amyloid fibrils, which is responsible for many neurodegenerative diseases including Alzheimer's disease (AD). In our previous study, synthesis and characterization of star‐shaped poly(D,L‐lactide)‐ b ‐gelatin (ss‐pLG) have been reported. In the present work, we have extended our work to study ss‐pLG against protein aggregation. To the best of our knowledge, this is the first report on the inhibition of amyloid fibrillation by protein grafted poly(D,L‐lactide). Bovine serum albumin (BSA) was chosen as the model protein, which readily forms fibril under high temperature. We found that ss‐pLG efficiently suppressed the fibril formation of BSA compared with gelatin (Gel), which was supported by Thioflavin T assay, circular dichroism (CD) spectroscopy and atomic force microscopy (AFM). In addition, ss‐pLG significantly curtailed amyloid‐induced hemolysis. We also found that incubation of ss‐pLG with neuroblastoma cells (MC65) protected the cells from fibril‐induced toxicity. The rescuing efficiency of ss‐pLG was better than Gel, which could be attributed to the reduced lamella thickness in branched ss‐pLG. These results suggest the significance of gelatin grafting, which probably allows gelatin to interact with the key residues of the amyloidogenic core of BSA effectively.