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Dr. Takahiro Muraoka, Kota Adachi, Dr. Mihoko Ui, Shunichi Kawasaki, Dr. Nabanita Sadhukhan, Haruki Obara, Dr. Hidehito Tochio, Prof. Masahiro Shirakawa and Prof. Kazushi Kinbara A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation Angewandte Chemie International Edition 52

Version of Record online: 30 JAN 2013 | DOI: 10.1002/anie.201206563

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Part of the solution: A PEG with a discrete triangular structure exhibits hydrophilicity/hydrophobicity switching upon increasing temperatures, and suppresses the thermal aggregation of lysozyme to retain nearly 80 % of the enzymatic activity. CD and NMR spectroscopic studies revealed that, with the structured PEG, the higher-order structures of lysozyme persist at high temperature, and the native conformation is recovered after cooling.

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