The helical and tubular structures self-assembled from proteins have inspired scientists to design synthetic building blocks that can be "polymerized" into supramolecular polymers through coordinated noncovalent interactions. However, cooperative supramolecular polymerization from large, synthetic macromolecules remains a challenge because of the difficulty of controlling the structure and interactions of macromolecular monomers. Herein we report the synthesis of polypeptide-grafted comb polymers and the use of their tunable secondary interactions in solution to achieve controlled supramolecular polymerization. The resulting tubular supramolecular structures, with external diameters of hundreds of nanometers and lengths of tens of micrometers, are stable and resemble to some extent biological superstructures assembled from proteins. This study shows that highly specific intermolecular interactions between macromolecular monomers can enable the cooperative growth of supramolecular polymers. The general applicability of this strategy was demonstrated by carrying out supramolecular polymerization from gold nanoparticles grafted with the same polypeptides on the surface.

Controlled assembly of inorganic nanoparticles (NPs) into structurally defined supramolecular polymers will create nanomaterials with new collective properties. However, supramolecular polymerization of isotropic NPs remains a challenge because of the lack of anisotropic interactions in these monomers to undergo directional associations for the cooperative growth of supramolecular chains. Herein we report self-assembly behavior of poly(l-glutamic acid)-grafted gold NPs in solution and describe how combined attractive and repulsive interactions influence the shape and size of the resulting supramolecular assemblies. The study shows that the chain growth of supramolecular polymers can be achieved from the NP monomers and the process occurs in two distinct stages, with a slow nucleation step followed by a faster chain propagation step. The resulting supramolecular structures depend on both the grafting density of the poly(l-glutamic acid) on the NPs and the size of the NPs.

The acidic ionic liquid (IL) functionalized polymer (PDVB-SO3H-[C3vim][SO3CF3]) possesses abundant nanoporous structures, strong acid strength and unique capability for deconstruction of crystalline cellulose into sugars in ILs. The polymer shows much improved catalytic activities in comparison with mineral acids, homogeneous acidic ionic liquids and the acidic resins such as Amberlyst 15. The enhanced catalytic activity found in the polymer is attributed to synergistic effects between the strongly acidic group and the ILs grafted onto the polymer, which by itself is capable of breaking down the crystalline structures of cellulose. This study may help develop cost-effective and green routes for conversion of biomass to fuels.

The formation of polycatalytic enzyme complexes may enhance the effectiveness of enzymes due to improved substrate interaction and synergistic actions of multiple enzymes in proximity. Much effort has been made to develop highly efficient polycatalytic cellulase complexes by immobilizing cellulases on low-cost polymer or nanoparticle scaffolds, aiming at their potential applications in biomass conversion to fuels. However, some key cellulases carry out the hydrolytic reaction on crystalline cellulose in a directional, processive manner. A large, artificial polycatalytic complex is unlikely to undergo a highly coordinated motion to slide on the cellulose surface as a whole unit. The mechanism underlying the activity enhancements observed in some artificial cellulase complexes and the limit of this approach remain elusive. Herein, we report the synthesis of polycatalytic cellulase complexes bound to colloidal polymer nanoparticles with a magnetic core and describe their unique adsorption, hydrolytic activities, and motions on cellulose. The polycatalytic clusters of cellulases on colloidal polymers show an increased rate of hydrolytic reactions on cellulose, but this was observed mainly at relatively low cellulase-to-cellulose ratios. Enhanced efficiency is mainly attributed to increased local concentrations of cellulases on the scaffolds and their polyvalent interactions with cellulose. However, once bound, the polycatalytic complexes can only carry out reactions locally and are not capable of relocating to new sites rapidly due to their lack of long-range surface mobility and their extremely tight binding. The development of highly optimized polycatalytic complexes may arise by developing novel nanoscaffolds that induce concerted motion of the complex as a whole.

Polycatalytic enzyme complexes made by immobilization of industrial enzymes on polymer- or nanoparticle-based scaffolds are technologically attractive due to their recyclability and their improved substrate binding and catalytic activities. Herein, we report the synthesis of polycatalytic complexes by the immobilization of nonprocessive cellulases on the surface of colloidal polymers with a magnetic nanoparticle core and the study of their binding and catalytic activities. These polycatalytic cellulase complexes have increased binding affinity for the substrate. But due to their larger size, these complexes were unable to access to the internal surfaces of cellulose and have significantly lower binding capacity when compared to those of the corresponding free enzymes. Analysis of released soluble sugars indicated that the formation of complexes may promote the prospect of having consistent, multiple attacks on cellulose substrate. Once bound to the substrate, polycatalytic complexes tend to remain on the surface with very limited mobility due to their strong, multivalent binding to cellulose. Hence, the overall performance of polycatalytic complexes is limited by its substrate accessibility as well as mobility on the substrate surface.