Fullerene-Based Mimics of Biocatalysts Show Remarkable Activity and Modularity.


Gülseren G., Saylam A., Marion A. , Özçubukçu S.

ACS applied materials & interfaces, vol.13, no.38, pp.45854-45863, 2021 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 13 Issue: 38
  • Publication Date: 2021
  • Doi Number: 10.1021/acsami.1c11516
  • Title of Journal : ACS applied materials & interfaces
  • Page Numbers: pp.45854-45863
  • Keywords: fullerene, fullerenol, biocatalysis, enzyme mimic, amino acids, molecular dynamics, QM/MM, PEPTIDE NANOFIBERS, ARTIFICIAL ENZYMES, CATALYSIS, PROTEASES, ARCHITECTURE, ANTIBODIES, PROTEIN, SITES, TRIAD, ACID

Abstract

© 2021 American Chemical Society.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.