Journal
BIOMACROMOLECULES
Volume 18, Issue 5, Pages 1574-1581Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biomac.7b00164
Keywords
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Funding
- NSFC [51273063, 21476143]
- Fundamental Research Funds for the Central Universities
- 111 Project Grant [B08021]
- European Synchrotron Radiation Facility
- Shanghai Synchrotron Radiation Facility
- China Scholarship Council
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The immobilization of bovine serum albumins (BSA) onto cationic spherical polyelectrolyte brushes (SPB) consisting of a solid polystyrene (PS) core and a densely grafted poly(2-aminoethyl methacrylate hydrochloride) (PAEMH) shell was studied by small-angle X-ray scattering (SAXS). The observed dynamics of adsorption of BSA onto SPB by time-resolved SAXS can be divided into two stages. In the first stage (tens of milliseconds), the added proteins as inbetween bridge instantaneously caused the aggregation of SPB. Then BSA penetrated into the brush layer driven by electrostatic attractions, and reached equilibrium in the second stage (tens of seconds). The amount of BSA immobilized onto brush layer reached the maximum when pH was increased to about 6.1 and BSA concentration to 10 g/L. The cationic SPB were confirmed to provide stronger adsorption capacity for BSA compared to anionic ones.
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