TY - JOUR
T1 - A structured monodisperse PEG for the effective suppression of protein aggregation
AU - Muraoka, Takahiro
AU - Adachi, Kota
AU - Ui, Mihoko
AU - Kawasaki, Shunichi
AU - Sadhukhan, Nabanita
AU - Obara, Haruki
AU - Tochio, Hidehito
AU - Shirakawa, Masahiro
AU - Kinbara, Kazushi
PY - 2013/2/25
Y1 - 2013/2/25
N2 - 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.
AB - 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.
KW - enzymes
KW - macrocycles
KW - polyethylene glycol
KW - protein manipulation
KW - supramolecular chemistry
UR - http://www.scopus.com/inward/record.url?scp=84874238762&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84874238762&partnerID=8YFLogxK
U2 - 10.1002/anie.201206563
DO - 10.1002/anie.201206563
M3 - Article
C2 - 23361965
AN - SCOPUS:84874238762
SN - 1433-7851
VL - 52
SP - 2430
EP - 2434
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 9
ER -