Enzyme-directed assembly and manipulation of organic nanomaterials

Abstract

Enzymes are the prime protagonists in the chemistry of living organisms. As such, chemists and biologists have long been fascinated by the array of highly selective transformations possible under biological conditions that are facilitated by enzymecatalyzed reactions. Moreover, enzymes are involved in replicating, repairing and transmitting information in a highly selective and organized fashion through detection and signal amplification cascades. Indeed, because of their selectivity and potential for use outside of biological systems, enzymes have found immense utility in various biochemical assays and are increasingly finding applications in the preparation of small molecules. By contrast, the use of enzymatic reactions to prepare and build supramolecular and nanoscale materials is relatively rare. In this article, we seek to highlight efforts over the past 10 years at taking advantage of enzymatic reactions to assemble and manipulate complex soft, organic materials on the nanoscale. It is tantalizing to think of these processes as mimics of natural systems where enzymes are used in the assembly and transformation of the most complex nanomaterials known, for example, virus capsid assemblies and the myriad array of nanoscale biomolecular machinery.

Enzyme-Triggered Cargo Release from Methionine Sulfoxide Containing Copolypeptide Vesicles

“…1 Numerous ERMs have been developed based on hydrogel or micelle structures, which can be switched between assembled and disassembled forms using enzymes under mild conditions. 1,2 Although many different enzymes and substrates have been used in ERMs, most of these rely on bond formation or cleavage reactions that primarily employ proteases, nucleases, or kinases/phosphatases. Many ERMs also utilize specific peptide or oligonucleotide sequences as enzyme substrates, 1,2 which in turn increases the cost and complexity of ERM preparation.…”

“…1,2 Although many different enzymes and substrates have been used in ERMs, most of these rely on bond formation or cleavage reactions that primarily employ proteases, nucleases, or kinases/phosphatases. Many ERMs also utilize specific peptide or oligonucleotide sequences as enzyme substrates, 1,2 which in turn increases the cost and complexity of ERM preparation. To enable widespread use of ERMs in various applications, such as diagnostics, sensors, drug delivery, adaptive surfaces, and regenerative medicine, it would be advantageous to be able to create ERMs that respond to different classes of enzymatic reactions, and that can be prepared using atom economical, scalable methods.…”

Clinical and Biological Implications of the Tumor Microenvironment

“…These concepts illustrate how the changes in the tumor microenvironment can be exploited clinically to detect small tumors that are otherwise difficult to localize. Other methods using labeled nanoparticles which can unravel to release their cargos in protease-rich tumor stroma [74] and/ or antibodies to preferentially concentrate in areas where the tumor cells juxtapose to stromal components [43] are under active exploration in some laboratories.…”

Hierarchical Self-Assembly of Amino Acid Derivatives into Enzyme-Responsive Luminescent Gel

“…As one of the non-covalent interactions, π-π stacking is vital to accelerate the alliance of supramolecular compounds to provide self-assembled structures with high stability [24]. Up to now, a lot of research for enzyme-responsive systems has been reported [25][26][27][28][29]. For instance, Zhang and coworkers have constructed several polymers by the electrostatic interaction between components responsive to phosphatase or acetylcholine [30][31][32][33].…”