TY - JOUR
T1 - Design of Synthetic Polymer Nanoparticles That Facilitate Resolubilization and Refolding of Aggregated Positively Charged Lysozyme
AU - Nakamoto, Masahiko
AU - Nonaka, Tadashi
AU - Shea, Kenneth J.
AU - Miura, Yoshiko
AU - Hoshino, Yu
N1 - Funding Information:
Financial support from MEXT (23111716 and 25107726), JSPS (15J04705 and 15H05486) and ImPACT Goda-program is greatly appreciated.
Publisher Copyright:
© 2016 American Chemical Society.
PY - 2016/4/20
Y1 - 2016/4/20
N2 - Designed polymer hydrogel nanoparticles (NPs) capable of facilitating resolubilization and refolding of an aggregated protein, positively charged lysozyme, are prepared. NPs designed to interact strongly with denatured lysozyme and relatively weakly with native lysozyme, facilitated resolubilization and refolding of aggregated lysozyme. Such NPs could be prepared by copolymerizing optimized combinations and populations of functional monomers. The refolded lysozyme showed native conformation and enzymatic activity. Eleven grams of aggregated protein was refolded by 1 g of NPs. However, NPs having low affinity to denatured lysozyme and NPs having high affinity to both denatured and native lysozyme showed relatively low facilitation activity. Our results suggest a potential strategy for the design of artificial chaperones with high facilitating activity.
AB - Designed polymer hydrogel nanoparticles (NPs) capable of facilitating resolubilization and refolding of an aggregated protein, positively charged lysozyme, are prepared. NPs designed to interact strongly with denatured lysozyme and relatively weakly with native lysozyme, facilitated resolubilization and refolding of aggregated lysozyme. Such NPs could be prepared by copolymerizing optimized combinations and populations of functional monomers. The refolded lysozyme showed native conformation and enzymatic activity. Eleven grams of aggregated protein was refolded by 1 g of NPs. However, NPs having low affinity to denatured lysozyme and NPs having high affinity to both denatured and native lysozyme showed relatively low facilitation activity. Our results suggest a potential strategy for the design of artificial chaperones with high facilitating activity.
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U2 - 10.1021/jacs.5b12600
DO - 10.1021/jacs.5b12600
M3 - Article
C2 - 26891855
AN - SCOPUS:84964720150
SN - 0002-7863
VL - 138
SP - 4282
EP - 4285
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 13
ER -