Abstract
There is increasing interest in using serum albumin, the most abundant plasma protein, as a stabilizing agent in the context of nanomedicine. Using poly(vinyl amine)-stabilized polypyrrole nanoparticles as an example, we report a facile generic route to prepare serum albumin-nanoparticle conjugates via heterocoagulation. Time-resolved dynamic light scattering (DLS), disk centrifuge photosedimentometry (DCP), and circular dichroism (CD) spectroscopy studies confirm that bovine serum albumin (BSA) adsorbs rapidly onto the cationic poly(vinyl amine)-stabilized polypyrrole nanoparticles and suggest that the initial well-defined protein coronal is subsequently cross-linked via thiol-disulfide exchange. These BSA-nanoparticle conjugates were further characterized by X-ray photoelectron spectroscopy (XPS), aqueous electrophoresis, field emission scanning electron microscopy (FE SEM), and transmission electron microscopy (TEM). They exhibit excellent long-term colloidal stability under physiological conditions without further purification, suggesting strong irreversible adsorption by the BSA. Protein adsorption appears to be co-operative and both thermodynamic and mechanistic aspects were examined via aqueous electrophoresis, DCP, and DLS studies.
Original language | English (US) |
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Pages (from-to) | 8261-8279 |
Number of pages | 19 |
Journal | ACS Nano |
Volume | 6 |
Issue number | 9 |
DOIs | |
State | Published - Sep 25 2012 |
Externally published | Yes |
Keywords
- heterocoagulation
- polypyrrole nanoparticles
- protein adsorption
- protein-nanoparticle interactions
- serum albumin
ASJC Scopus subject areas
- General Materials Science
- General Engineering
- General Physics and Astronomy