Abstract
This paper presents a systematic study of bovine serum albumin (BSA) conjugation on the amine-functionalized magnetic nanoparticles (MNPs) and the effects of various experimental parameters on the conjugation process. The amine-functionalized Fe2O3 NPs with silica shell were synthesized through surface modification. The BSA conjugation on the amine-functionalized Fe2O3 NPs was achieved through covalent binding via carbodiimide activation. Morphology and magnetic properties of the nanoparticles were investigated. The influence of reaction time, the initial protein concentration, and the temperature on BSA conjugation was studied. The increased reaction time promoted the conjugation of BSA on the Fe2O3 NPs and finally reached the saturation at 43.4 mg/g. The initial BSA concentration can increase the amount of conjugated BSA. The temperature exhibited no significant effect on the conjugation process. The results are useful for designing effective fabrication strategy for protein-conjugated nanomaterials.
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