ACS Applied Materials & Interfaces · 2021 · 18 citations · 31 references
Natural SciencesBiotechnologyChemistryBiocatalysisCatalysisEnzymologyCatalyst DesignCatalytic MechanismsEnzymatic CatalysisEnzyme CatalysisEnzyme-substrate RecognitionNanocatalysisAmino Acid FunctionalizationAmino FunctionalizationArtificial Enzyme CatalysisBiocatalyst DesignBiomolecule-inorganic HybridsCatalytic ActivityCatalytic Activity EnhancementCatalytic Hybrid Materials
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 fullerene nanocatalysts, and that emulates enzymatic active sites through multifunctional self-assembled nanostructures. As a proof-of-concept, 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.
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Short peptides self-assemble to produce catalytic amyloids
Caroline M. Rufo, Yurii S. Moroz, O.V. Moroz et al. · Nature Chemistry · 2014 · 657 citations · Full text