A structured monodisperse PEG for the effective suppression of protein aggregation.
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.
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Sendai, Japan.
Takahiro
T
Muraoka
Kota
K
Adachi
Mihoko
M
Ui
Shunichi
S
Kawasaki
Nabanita
N
Sadhukhan
Haruki
H
Obara
Hidehito
H
Tochio
Masahiro
M
Shirakawa
Kazushi
K
Kinbara
D008958:Models, Molecular; D011092:Polyethylene Glycols / Q000737:chemistry*; D011487:Protein Conformation; D055503:Protein Multimerization; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D011092:Polyethylene Glycols