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

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...

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Detalles Bibliográficos
Autores principales: Lenzen, Karst, Planchestainer, Matteo, Feller, Isabelle, Padrosa, David Roura, Paradisi, Francesca, Albrecht, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2021
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427656/
https://www.ncbi.nlm.nih.gov/pubmed/34498652
http://dx.doi.org/10.1039/d1cc03158a
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author Lenzen, Karst
Planchestainer, Matteo
Feller, Isabelle
Padrosa, David Roura
Paradisi, Francesca
Albrecht, Martin
author_facet Lenzen, Karst
Planchestainer, Matteo
Feller, Isabelle
Padrosa, David Roura
Paradisi, Francesca
Albrecht, Martin
author_sort Lenzen, Karst
collection PubMed
description 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.
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spelling pubmed-84276562021-09-27 Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity Lenzen, Karst Planchestainer, Matteo Feller, Isabelle Padrosa, David Roura Paradisi, Francesca Albrecht, Martin Chem Commun (Camb) Chemistry 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. The Royal Society of Chemistry 2021-08-06 /pmc/articles/PMC8427656/ /pubmed/34498652 http://dx.doi.org/10.1039/d1cc03158a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/
spellingShingle Chemistry
Lenzen, Karst
Planchestainer, Matteo
Feller, Isabelle
Padrosa, David Roura
Paradisi, Francesca
Albrecht, Martin
Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title_full Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title_fullStr Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title_full_unstemmed Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title_short Minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
title_sort minimalistic peptidic scaffolds harbouring an artificial carbene-containing amino acid modulate reductase activity
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427656/
https://www.ncbi.nlm.nih.gov/pubmed/34498652
http://dx.doi.org/10.1039/d1cc03158a
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