Abstract
The dependence of the aggregation of magnetic iron oxide nanoparticles in aqueous suspensions under the action of human serum albumin is analyzed based on the data of proton magnetic relaxation. It is shown that albumin adsorption on magnetic nanoparticles gives rise to the formation of a protein corona and clusters of magnetic nanoparticles, decreasing the aggregation stability of the suspension in a 7.1-T magnetic field. Clustering of magnetic iron oxide nanoparticles enhances the relaxation efficiency of magnetic suspensions during NMR measurements.
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