Nitric oxide producing artificial enzymes based on metalloporphyrins

X. Qian, M. A. Ramos-Docampo, C. Ade, E. Brodszkij, I. N. Westensee, B. Städler*

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Abstract

Artificial enzymes are synthetic materials or molecules that exhibit enzyme-like activities. Herein, we report artificial enzymes based on metalloporphyrins (MPs) that can mimic nitric oxide synthase (NOS) to produce nitric oxide (NO) from L-arginine (Arg) using hydrogen peroxide (H2O2) as an oxidant, and we determine the microenvironmental influence on their activity and stability. An assortment of structurally diverse water-soluble MPs was synthesized, and their NO production was compared. Improved catalytic activity and stability of the lead MP were observed when it was conjugated to the hydrophilic homopolymer poly(2-carboxyethyl acrylate) (PCEA). Micelles assembled from the amphiphilic block copolymer poly(cholesteryl methacrylate)-block-PCEA functionalized with the lead MP, and MP-conjugated PCEA polymer chains immobilized on silica particles resulted in moieties with ∼3× higher catalytic activity compared to the monomeric MP. Finally, the PCEA-coated silica particles could use the MPs as motor units to exhibit enhanced diffusion in the presence of the required fuel molecules Arg and H2O2. Taken together, the microenvironments of the artificial enzymes have a marked impact on their activity and stability, and these NO-producing MPs offer an interesting synthetic alternative to their natural counterparts.

Original languageEnglish
Article number100743
JournalMaterials Today Chemistry
Volume23
Number of pages11
DOIs
Publication statusPublished - Mar 2022

Keywords

  • Enzyme mimic
  • Locomotion
  • Metalloporphyrin
  • Nitric oxide production

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