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Please use this identifier to cite or link to this item: http://hdl.handle.net/10119/13537

Title: A zwitterionic polymer as a novel inhibitor of protein aggregation
Authors: Rajan, Robin
Matsumura, Kazuaki
Issue Date: 2015-06-19
Publisher: Royal Society of Chemistry
Magazine name: Journal of Materials Chemistry B
Volume: 3
Number: 28
Start page: 5683
End page: 5689
DOI: 10.1039/C5TB01021G
Abstract: We report the novel one-step synthesis of a zwitterionic polymer, poly-sulfobetaine, via living reversible addition fragmentation chain transfer (RAFT) polymerization. Lysozyme did not aggregate when heated in presence of this polymer. Amyloid formation, the cause of many diseases, was also suppressed. The zwitterionic polymer was significantly more efficient than previously described inhibitors of protein aggregation. Lysozyme heated in the presence of polysulfobetaine retained its solubility and very high enzymatic efficiency, even after prolonged heating. The secondary structures of lysozyme change with increasing temperature, accompanied by an increase in β-structure. This change was prevented by mixing the polymer with lysozyme. ^1H-NMR before and after aggregation revealed the conformational changes taking place in the lysozyme: during aggregation, lysozyme is transformed into a random coil conformation, thus losing its secondary structure. Presence of the polymer facilitates retention of partial higher order structures and lysozyme solubility at higher temperatures. The high efficiency of the polyampholyte was ascribed to its ability to prevent collisions between aggregating species by acting as molecular shield.
Rights: Copyright (C) 2015 Royal Society of Chemistry. Robin Rajan and Kazuaki Matsumura, Journal of Materials Chemistry B, 3(28), 2015, 5683-5689. http://dx.doi.org/10.1039/C5TB01021G - Reproduced by permission of The Royal Society of Chemistry
URI: http://hdl.handle.net/10119/13537
Material Type: author
Appears in Collections:c10-1. 雑誌掲載論文 (Journal Articles)

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