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このアイテムの引用には次の識別子を使用してください: http://hdl.handle.net/10119/18768

タイトル: Polyethylene-glycol-modified Zwitterionic Polymers assisted Protein Aggregation Arrest and Refolding
著者: Debas, Alisha
Matsumura, Kazuaki
Rajan, Robin
発行日: 2022-07-05
出版者: Royal Society of Chemistry
誌名: Molecular Systems Design & Engineering
巻: 7
号: 10
開始ページ: 1327
終了ページ: 1335
DOI: 10.1039/D2ME00084A
抄録: Protein aggregation limits the development of protein-based drugs, and leads to neurological disorders. In this study, the zwitterionic polymer, poly-sulfobetaine (p-SPB), was modified using the polyethylene glycol (PEG), and exhibited the remarkable suppression of heat-induced lysozyme aggregation. The study revealed that the modified polymers prevented the formation of amyloid fibrils, and retained the enzymatic activity of the lysozyme, which is lost after heating. An increase in the molecular weight of the polymers afforded higher efficacy to perpetuate enzymatic activity. Along with the effectiveness of these polymers for lysozyme aggregation arrest, further evaluations revealed that these polymers facilitated the refolding of protein because of their tendency to dissolve the already formed fibrils, and regained the lost lysozyme activity. These findings suggest that the amalgamation of PEG and p-SPB has the potential to protect proteins from aggregation via altering the hydrophobic environment of the lysozyme, creating a molecular shield around the protein molecules, and thus, providing scope for the development of protein-based biopharmaceuticals.
Rights: This is the author's version of the work. Copyright (C) 2022 Royal Society of Chemistry. Reproduced from Alisha Debas, Kazuaki Matsumura and Robin Rajan, Molecular Systems Design & Engineering, 7 (10), 2022, 1327-1335, with permission from Institution of Chemical Engineers (IChemE) and the Royal Society of Chemistry. DOI: 10.1039/D2ME00084A
URI: http://hdl.handle.net/10119/18768
資料タイプ: author
出現コレクション:c10-1. 雑誌掲載論文 (Journal Articles)

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