The design of catalysts with greater control over catalytic activity and stability is a major challenge with substantial impact on fundamental chemistry and industrial applications. Due to their unparalleled diversity, selectivity, and efficiency, enzymes are promising models for next-generation catalysts, and considerable efforts have been devoted to incorporating the principles of their mechanisms of action into artificial systems. We report a heretofore undocumented catalyst design that introduces fullerenes to the field of biocatalysis, which we refer to as f ullerene nanocatalysts, and that emulates enzymatic active sites through multifunctional self-assembled nanostructures. As a proof-ofconcept, we mimicked the reactivity of hydrolases using fullerene nanocatalysts functionalized with the basic components of the parent enzyme with remarkable activity. Owing to the versatile amino acid-based functionalization repertoire of fullerene nanocatalysts, these next-generation carbon/biomolecule hybrids have potential to mimic the activity of other families of enzymes and, therefore, offer new perspectives for the design of biocompatible, high-efficiency artificial nanocatalysts.

This study presents the comparative cell attachment investigation of TAT and well-known RGD peptide modified surfaces.

Enzyme mimicry is a topic of considerable interest in the development of multifunctional biomimetic materials. Mimicking enzyme activity is a major challenge in biomaterials research, and artificial analogs that simultaneously recapitulate the catalytic and metabolic activity of native enzymes are considered to be the ultimate goal of this field. This consensus may be challenged by self‐assembling multifunctional nanostructures to develop close‐to‐fidelity enzyme mimics. Here, the ability of fullerene nanostructures decorated with active units to form enzyme‐like materials that can mimic phosphatases in a metal‐free manner is presented. These nanostructures self‐assemble into nanoclusters forming multiple random active sites that can cleave both phosphomonoesters and phosphodiesters while being more specific for the phosphomonoesters. Moreover, they are reusable and show an increase in catalytic activity over multiple cycles similar to their natural counterparts. In addition to having enzyme‐like catalytic properties, these nanocatalysts imitate the biological functions of their natural analogs by inducing biomineralization and osteoinduction in preosteoblast and mesenchymal stem cells in vitro studies.

Peptide nucleic acids are synthetic molecules crafted to mimic natural nucleic acids, and thus, they are widely utilized in many chemical, and, biomedical applications. Although there exist many approaches to synthesize monomers to date, there is still room to improve these methodologies. With this motivation, we compared some widely utilized synthetic routes to obtain N-Boc-PNA-T-OH, and N-Fmoc-PNA-T-OH. Our results indicate that N-Bocethylenediamine is the most pivotal intermediate in the chemistry of PNA, and synthetic route commencing with this material affords these two PNA monomers in relatively high yield, and purity, while being very reproducible.