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


ABSTRACT: 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.

SUBMITTER: Lenzen K 

PROVIDER: S-EPMC8427656 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature

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

Lenzen Karst K   Planchestainer Matteo M   Feller Isabelle I   Padrosa David Roura DR   Paradisi Francesca F   Albrecht Martin M  

Chemical communications (Cambridge, England) 20210909 72


Inspired by the boom of new artificial metalloenzymes, we developed an Fmoc-protected histidinium salt (Hum) as N-heterocyclic carbene precursor. Hum was placed <i>via</i> 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. ...[more]

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