| 초록 |
We describe a simple method for the construction and control of polymer-protein hybrid spherical aggregates in situ from nickel complexed (nitrilotriacetic acid)-end-functionalized polystyrene (Ni-NTA-PS) and histidine-tagged green fluorescent protein (His-tagged GFP) through NTA-Ni/His interaction in water/DMF (DMF 4 vol. %) at physiological pH. The generality of the approach was demonstrated by using His-tagged GFP and His-tagged lipases. Transmission electron microscopy (TEM) and dynamic light scattering (DLS) measurements revealed that hybrid aggregates of His-tagged GFP were stable up to 15 days. The size of hybrid aggregates depended on the molecular weight of polymers, concentration of polymers, concentration of protein, and also the rate of adding polymer to solvent, containing protein. A possible mechanism for the formation of such polymer-protein hybrid aggregates is also described. |
