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

Autor: Lenzen K; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch., Planchestainer M; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch., Feller I; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch., Padrosa DR; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch., Paradisi F; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch., Albrecht M; Department of Chemistry, Biochemistry & Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland. Francesca.paradisi@dcb.unibe.ch.
Jazyk: angličtina
Zdroj: Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2021 Sep 09; Vol. 57 (72), pp. 9068-9071. Date of Electronic Publication: 2021 Sep 09.
DOI: 10.1039/d1cc03158a
Abstrakt: 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.
Databáze: MEDLINE
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