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A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation
Author(s) -
Muraoka Takahiro,
Adachi Kota,
Ui Mihoko,
Kawasaki Shunichi,
Sadhukhan Nabanita,
Obara Haruki,
Tochio Hidehito,
Shirakawa Masahiro,
Kinbara Kazushi
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201206563
Subject(s) - lysozyme , peg ratio , dispersity , chemical engineering , chemistry , protein aggregation , biophysics , crystallography , materials science , polymer chemistry , biochemistry , business , biology , finance , engineering
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.