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Photothermal conversion (PTC) nanostructures have great potential for applications in many fields, and therefore, they have attracted tremendous attention. However, the construction of a PTC nanoreactor with multi-compartment structure to achieve the combination of unique chemical properties and structural feature is still challenging due to the synthetic difficulties. Herein, we designed and synthesized a catalytically active, PTC gold (Au)@polydopamine (PDA) nanoreactor driven by infrared irradiation using assembled PS-b-P2VP nanosphere as soft template. The particles exhibit multi-compartment structure which is revealed by 3D electron tomography characterization technique. They feature permeable shells with tunable shell thickness. Full kinetics for the reduction reaction of 4-nitrophenol has been investigated using these particles as nanoreactors and compared with other reported systems. Notably, a remarkable acceleration of the catalytic reaction upon near-infrared irradiation is demonstrated, which reveals for the first time the importance of the synergistic effect of photothermal conversion and complex inner structure to the kinetics of the catalytic reduction. The ease of synthesis and fresh insights into catalysis will promote a new platform for novel nanoreactor studies.
We discuss recent investigations of the interaction of polyelectrolytes with proteins. In particular, we review our recent studies on the interaction of simple proteins such as human serum albumin (HSA) and lysozyme with linear polyelectrolytes, charged dendrimers, charged networks, and polyelectrolyte brushes. In all cases discussed here, we combined experimental work with molecular dynamics (MD) simulations and mean-field theories. In particular, isothermal titration calorimetry (ITC) has been employed to obtain the respective binding constants K-b and the Gibbs free energy of binding. MD simulations with explicit counterions but implicit water demonstrate that counterion release is the main driving force for the binding of proteins to strongly charged polyelectrolytes: patches of positive charges located on the surface of the protein become multivalent counterions of the polyelectrolyte, thereby releasing a number of counterions condensed on the polyelectrolyte. The binding Gibbs free energy due to counterion release is predicted to scale with the logarithm of the salt concentration in the system, which is verified by both simulations and experiment. In several cases, namely, for the interaction of proteins with linear polyelectrolytes and highly charged hydrophilic dendrimers, the binding constant could be calculated from simulations to very good approximation. This finding demonstrated that in these cases explicit hydration effects do not contribute to the Gibbs free energy of binding. The Gibbs free energy can also be used to predict the kinetics of protein uptake by microgels for a given system by applying dynamic density functional theory. The entire discussion demonstrates that the direct comparison of theory with experiments can lead to a full understanding of the interaction of proteins with charged polymers. Possible implications for applications, such as drug design, are discussed.