Journal
LANGMUIR
Volume 28, Issue 24, Pages 9131-9139Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la3005213
Keywords
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Funding
- Robert A. Welch Foundation [C-1664]
- Cancer Prevention and Research Institute of Texas [CPRIT] [RP110355]
- Rice University
- National Science Foundation [CBET-1134417, CHE-1151647]
- National Institutes of Health [GM94246-01A1]
- Royal Thai Government
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1151647] Funding Source: National Science Foundation
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1134417] Funding Source: National Science Foundation
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We present in situ observations of adsorption of bovine serum albumin (BSA) on citrate-stabilized gold nanospheres. We implemented scattering correlation spectroscopy as a tool to quantify changes in the nanoparticle Brownian motion resulting from BSA adsorption onto the nanoparticle surface. Protein binding was observed as an increase in the nanoparticle hydrodynamic radius. Our results indicate the formation of a protein monolayer at similar albumin concentrations as those found in human blood. Additionally, by monitoring the frequency and intensity of individual scattering,events caused by single gold nanoparticles passing the observation volume, we found that BSA did not induce colloidal aggregation, a relevant result from the toxicological viewpoint. Moreover, to elucidate the thermodynamics of the gold nanoparticle BSA association, we measured an adsorption isotherm which was best described by an anticooperative binding model. The number of binding sites based on this model was consistent with a BSA monolayer in its native state. In contrast, experiments using poly(ethylene glycol)-capped gold nanoparticles revealed no evidence for adsorption of BSA.
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