TY - JOUR
T1 - Protein Nanoparticle Formation Using a Circularly Permuted α-Helix-Rich Trimeric Protein
AU - Kawakami, Norifumi
AU - Kondo, Hiroki
AU - Muramatsu, Masayuki
AU - Miyamoto, Kenji
N1 - Funding Information:
ACKNOWLEDGMENTS The authors wish to acknowledge the Division for Medical Research Engineering, Nagoya University Graduate School of Medicine, for the technical support of TEM observation. This work was supported by Keio Gijuku Academic Development Funds to N.K. from Keio University.
Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/2/15
Y1 - 2017/2/15
N2 - We here report the production of highly spherical protein nanoparticles based on the domain-swapping oligomerization of a circularly permuted trimeric protein, major histocompatibility complex (MHC) class II associated chaperonin. The size distribution of the nanoparticles can be adjusted to between 40 and 100 nm in diameter, and thus, these particles are suitable as drug carriers following purification under basic conditions. Our approach involves no harsh treatments and could provide an alternative approach for protein nanoparticle formation.
AB - We here report the production of highly spherical protein nanoparticles based on the domain-swapping oligomerization of a circularly permuted trimeric protein, major histocompatibility complex (MHC) class II associated chaperonin. The size distribution of the nanoparticles can be adjusted to between 40 and 100 nm in diameter, and thus, these particles are suitable as drug carriers following purification under basic conditions. Our approach involves no harsh treatments and could provide an alternative approach for protein nanoparticle formation.
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U2 - 10.1021/acs.bioconjchem.6b00735
DO - 10.1021/acs.bioconjchem.6b00735
M3 - Article
C2 - 28090773
AN - SCOPUS:85013046179
SN - 1043-1802
VL - 28
SP - 336
EP - 340
JO - Bioconjugate Chemistry
JF - Bioconjugate Chemistry
IS - 2
ER -