ABSTRACT
Complexation between oppositely charged nanoparticles (NPs) and polyelectrolytes (PEs) is a scalable approach to assemble functional, stimuli-responsive membranes. Complexation at interfaces of aqueous two-phase systems (ATPSs) has emerged as a powerful method to assemble these functional structures. Membranes formed at these interfaces can grow continuously to thicknesses approaching several millimeters and display a high degree of tunability via modification of solution properties such as ionic strength. To identify the membrane assembly mechanism, we study interfacial assembly in a prototypical dextran/PEG ATPS, in which silica (SiO2) NPs suspended in the PEG phase undergo interfacial complexation with poly(diallyldimethylammonium chloride) (PDADMAC) supplied in the dextran phase. Using a microfluidic device that facilitates sequential insertion of fluorescent and nonfluorescent PDADMAC, we observe a transition in the membrane growth mechanism with ionic strength. In the absence of added salt ([NaCl] = 0 mM) PDADMAC chains permeate through the existing membrane to complex with NPs on the PEG side of the membrane, leading to the formation of well-stratified structures. At elevated ionic strength ([NaCl] = 500 mM), this permeation mechanism is lost. Rather, the complexing species incorporate uniformly across the membrane. We attribute this transition to a rapid exchange of PE-counterion, NP-counterion, and PE/NP binding sites facilitated by an increase in extrinsically compensated charged groups on the NPs and PEs at high salinity. These PDADMAC/SiO2 NP membranes have tremendous potential for the formation of functional membranes, offering control over the internal structure and serving as an ideal system for the generation of targeted release systems.
ABSTRACT
Active biocompatible systems are of great current interest for their possible applications in drug or antidote delivery at specific locations. Herein, we report the synthesis and study of self-propelled microparticles powered by enzymatic reactions and their directed movement in substrate concentration gradient. Polystyrene microparticles were functionalized with the enzymes urease and catalase using a biotin-streptavidin linkage procedure. The motion of the enzyme-coated particles was studied in the presence of the respective substrates, using optical microscopy and dynamic light scattering analysis. The diffusion of the particles was found to increase in a substrate concentration dependent manner. The directed chemotactic movement of these enzyme-powered motors up the substrate gradient was studied using three-inlet microfluidic channel architecture.
