Document Type
Article
Publication Date
3-25-2019
Publication Title
Canadian Journal of Chemistry
Volume
97
Issue
8
First Page
577
Keywords
Magnetite nanoparticles, bovine serum albumin, Langmuir isotherm, adsorption kinetics, adsorption thermodynamics
Last Page
583
Abstract
Bare, uncoated magnetite nanoparticles, synthesized using an electrochemical surfactant-free synthesis, have highly oxidized surfaces that prevent aggregation. These particles have demonstrated highly intriguing biological activity showing extremely potent antibiotic activity against both gram-positive and gram-negative bacteria with little toxicity to rats. This difference in activity could be ascribed to the nature of the protein corona. In this study the kinetics and thermodynamics of the binding of bovine serum albumin, used as a model serum protein, to these magnetite nanoparticles was analyzed. There is no significant change in particle diameter by dynamic light scattering following adsorption indicating corona formation does not induce aggregation. The maximum adsorption capacity of the particles was determined to be 300 mg of BSA/g of magnetite. The particles are able to adsorb 90% of the BSA at protein concentrations as high as 500 mg/L. The adsorption is best described using a pseudo-second-order model and a Langmuir Type III isotherm model. Thermodynamic analysis showed that the process is entropically driven and is spontaneous at all tested temperatures and conditions. However, it appears to be a weak to moderate physical adsorption. This moderate binding affinity could indicate the differential biological activity of these particles towards bacteria and mammalian cells and further support the contention that these are potentially useful new tools for targeting antibiotic-resistant bacteria.
DOI
10.1139/cjc-2019-0008
Funding Reference Number
NSERC, 2018-06338
Recommended Citation
Rahdar, Somayeh; Rahdar, Abbas; Ahmadi, Shahin; and Trant, John F.. (2019). Adsorption of bovine serum albumin (BSA) by bare magnetite nanoparticles with surface oxidative impurities that prevent aggregation. Canadian Journal of Chemistry, 97 (8), 577-583.
https://scholar.uwindsor.ca/chemistrybiochemistrypub/142