Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity

Autor: David Roura Padrosa, Francesca Paradisi, Karst Eelco Lenzen, Isabelle Feller, Matteo Planchestainer, Martin Albrecht
Rok vydání: 2021
Předmět:
Zdroj: Lenzen, Karst; Planchestainer, Matteo; Feller, Isabelle; Roura Padrosa, David; Paradisi, Francesca; Albrecht, Martin (2021). Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity. Chemical communications, 57(72), pp. 9068-9071. Royal Society of Chemistry 10.1039/D1CC03158A
Chemical Communications (Cambridge, England)
DOI: 10.48350/159393
Popis: Inspired by the boom of new artificial metalloenzymes, we developed an Fmoc-protected histidinium salt (Hum) as N-heterocyclic carbene precursor. Hum was placed via solid-phase peptide synthesis into short 7-mer peptides. Upon iridation, the metallo-peptidic construct displayed activity in catalytic hydrogenation that outperforms small molecule analogues and which is dependent on the peptide sequence, a typical feature of metalloenzymes.
A non-natural histidinium amino acid has been developed and used for solid-phase peptide synthesis to construct a peptide iridium carbene conjugate as artificial mini-peptide for hydrogenation catalysis.
Databáze: OpenAIRE