Nanoparticle-supported temperature responsive polymer brushes for affinity separation of histidine-tagged recombinant proteins

Lingdong Jiang, Lei Ye

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review


We developed a modular approach for the preparation of nanoparticle-supported polymer brushes carrying repeating iminodiacetate units for affinity separation of histidine-tagged recombinant proteins. The nanoparticle-supported polymer brushes were prepared via the combination of surface-initiated atom transfer radical polymerization with Cu(I)-catalyzed azide–alkyne cycloaddition reaction. The nanocomposite materials were characterized to determine the particle size, morphology, organic content, densities of polymer chains and the affinity ligand. Protein binding assay illustrated that the iminodiacetate-rich polymer brushes enable to selectively bind histidine-tagged recombinant proteins in the presence of abundant interfering proteins. More importantly, the protein binding capacity can be tuned by adjusting the environmental temperature. Statement of Significance: The nanoparticle core-polymer brush structure enables selective binding of histidine-tagged recombinant proteins via multiple metal-coordination interactions. The soft and flexible structure of the polymer brushes was found beneficial for lowering the steric hindrance in protein binding. Taking advantage of the conformational changes of the polymer brushes at different temperatures, it is possible to modulate the protein binding on the nanocomposite by adjusting the environmental temperature. In general, the iminodiacetate-rich core-brush nano adsorbents are attractive for purifying histidine-tagged recombinant proteins practically. The synthetic approach reported here may be expanded to develop other advanced functional materials for applications in various biomedical fields ranging from biosensors to drug delivery.

Sidor (från-till)447-458
TidskriftActa Biomaterialia
Tidigt onlinedatum2019
StatusPublished - 2019

Ämnesklassifikation (UKÄ)

  • Strukturbiologi


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