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Analysis of size-dependent protein adsorption behavior of iminodiacetic acid functionalized superparamagnetic iron oxide nanoparticles(IDA-SPION)

초록

영어

Superparamagnetic iron oxide particles functionalized with iminodiacetic acid (IDA-SPION) with varying diameters ranging from 350 to 450 nm were synthesized by covalently grafting GLYMO-IDA on silica coated iron oxide superparamagnetic nanoparticles (silica coated SPION). The size and/or ligand density of IDA-SPION is adjustable by changing the parameters (i.e. sonication time to disperse magnetite growth seed or TEOS addition rate) during the sol-gel based synthesis process. Cu2+-charged IDA-SPION (Cu2+-IDA-SPION) exhibits size and metal ion ligand density dependent binding affinity and capacity for a model protein, bovine serum albumin (BSA). As the size of Cu2+-IDA-SPION increases, higher maximum BSA adsorption capacity (Qm) and dissociation constant (Kd) are exhibited, indicating that the increase in BSA adsorption capacity is coupled with compromised affinity towards the target protein.1 This research provides an insight to synthesizing IDA-SPIONs with controllable size and protein adsorption property, thereby providing a simple method capable of addressing the various requirements in a wide range of protein purification or impurity removal applications.

저자정보

  • Dongkwan KIM School of Chemical Engineering, Sungkyunkwan University, 300 Chunchun-dong, Suwon, Kyeonggi-do 440-746, Korea.
  • Lihan TAN Department of Chemical &Biomolecular Engineering, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260.
  • Woo-Seok CHOE School of Chemical Engineering, Sungkyunkwan University, 300 Chunchun-dong, Suwon, Kyeonggi-do 440-746, Korea.

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