Chemical modification of dehydrated amino acids in natural antimicrobial peptides by photoredox catalysis

Dowine de Bruijn, Gerard Roelfes

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20 Citations (Scopus)
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Abstract

Dehydroalanine (Dha) and dehydrobutyrine (Dhb) are remarkably versatile non-canonical amino acids often found in antimicrobial peptides. Here, we present the selective modification of Dha and Dhb in antimicrobial peptides via photocatalytic activation of organoborates under influence of visible light. Ir(dF(CF3)ppy)2(dtbbpy)PF6 was used as photoredox catalyst in aqueous solutions for the modification of thiostrepton and nisin. The mild conditions and high selectivity for the dehydrated residues, show photoredox catalysis is a promising tool for modification of peptide derived natural products.

Original languageEnglish
Pages (from-to)11314-11318
JournalChemistry
Volume24
Issue number44
Early online date25-Jun-2018
DOIs
Publication statusPublished - 6-Aug-2018

Keywords

  • bio-orthogonal catalysis
  • dehydroalanine
  • nisin
  • photoredox catalysis
  • thiostrepton
  • SITE
  • DEHYDROALANINE
  • CHEMISTRY
  • PROTEINS
  • NISIN
  • BIOSYNTHESIS
  • THIOSTREPTON
  • ARYLATION
  • CYSTEINE
  • ANALOGS

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