Nanogels prepared by self-assembly of oppositely charged globular proteins.
Ovalbumin and lysozyme are two main proteins in hen egg white with the isoelectric points of 4.8 and 11, respectively. Herein we report the manufacture of stable, narrowly distributed nanogels (hydrodynamic radius about 100 nm) using a novel and convenient method: ovalbumin and lysozyme solutions were mixed at pH 5.3, the mixture solution was adjusted to pH 10.3, then subsequently stirred and heated. The nanogels were characterized using a combination of techniques. The nanogels have spherical shape and core-shell structure. The core is mainly composed of lysozyme and the shell is mainly composed of ovalbumin. The proteins in the nanogels are in denatured states and they are bound by intermolecular hydrophobic interactions, hydrogen bonds, and disulfide bonds. The charges of the nanogels can be modulated by the pH of the medium. The electrostatic repulsion of ovalbumin molecules on the nanogel surface stabilizes the nanogels in aqueous solution. The formation mechanism of the nanogels is discussed.
Yu
Shaoyong
S
The Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200433, China.
Yao
Ping
P
Jiang
Ming
M
Zhang
Guangzhao
G
D006358:Hot Temperature; D020100:Hydrogels / Q000138:chemical synthesis* / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008027:Light; D008564:Membrane Potentials; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010047:Ovalbumin / Q000737:chemistry* / Q000378:metabolism*; D012542:Scattering, Radiation; D012996:Solutions / Q000737:chemistry; D013997:Time Factors; D014867:Water / Q000737:chemistry
D020100:Hydrogels; D012996:Solutions; D014867:Water; D010047:Ovalbumin; D009113:Muramidase