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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.
Afiliação
  • 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.
Chem Commun (Camb) ; 57(72): 9068-9071, 2021 Sep 09.
Article em En | MEDLINE | ID: mdl-34498652
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.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Peptídeos / Aminoácidos / Metano Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Suíça

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Oxirredutases / Peptídeos / Aminoácidos / Metano Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Suíça