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A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation


  • We thank Prof. K. Tsumoto (University of Tokyo) for fruitful discussions. This work was partially supported by the Ministry of Education, Science, Sports and Culture (Japan), Grants-in-Aid for Young Scientists S (21675003 for K.K.), Scientific Research on Innovative Areas “Spying minority in biological phenomena (No. 3306)” (23115003 for K.K.), and Exploratory Research (24655112 for T.M.) and the Management Expenses Grants for National Universities Corporations from the Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT).


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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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