Assembled protein-based substances are emerging and promising classes of materials that provide unique properties for various applications in biotechnology and nanotechnolegy. Self-assembly is an effective way to immobilize protein. In this study, DNAs-conjugated bovine serum albumin （BSA） assembled into fibers via DNA hybridization is demonstrated. The morphology of fibers was observed by optical microscopy, scanning electron microscopy （SEM）, and atomic force microscopy （AFM）, and the assembly mechanism was then analysed and discussed. BSA molecules were first linked by DNA molecule and formed linear chains. These chains then were parallelly linked through additional DNA hybridization. Finally, several BSA chains further assembled into fibers by layering lamellae in a parallel manner. This work perhaps will provide a guide to the immobilization of enzyme, which could be applied to increase its catalytic efficiency in biomedicine and nanotechnology.
A series of multicomponent hydrogels were prepared by the copolymerization of hydrophobic silicon-containing monomer 3-bis（trimethylsilyloxy） methylsilylpropyl glycerol methacrylate（Si MA） with the solvent-responsive monomers 2-hydroxyethyl methacrylate（HEMA） and N-vinyl pyrrolidone（NVP） and thermosensitive monomer N,N-dimethyl acrylamide（DMA）. 2-Hydroxy-2-methyl phenyl acetone（D-1173） was chosen as UV initiator and five different dienes/triene monomers were selected as crosslinking agent in order to select the best crosslinker. The ethanol extraction experiments as well as the FTIR, DSC and TG results showed that the copolymerization was effective. The optical, permeability, and mechanical analysis results demonstrated that the obtained hydrogels were highly transparent with good oxygen permeability and mechanical properties. And the impact of crosslinker on the mechanical properties of the hydrogels was also discussed in detail. The basic results demonstrated that the obtained hydrogels had good stimuli-responsive effects to both p H value and solvent.
