A Water-Soluble Iridium Photocatalyst for Chemical Modification of Dehydroalanines in Peptides and Proteins.

ABSTRACT: Dehydroalanine (Dha) residues are attractive noncanonical amino acids that occur naturally in ribosomally synthesised and post-translationally modified peptides (RiPPs). Dha residues are attractive targets for selective late-stage modification of these complex biomolecules. In this work, we show the selective photocatalytic modification of dehydroalanine residues in the antimicrobial peptide nisin and in the proteins small ubiquitin-like modifier (SUMO) and superfolder green fluorescent protein (sfGFP). For this purpose, a new water-soluble iridium(III) photoredox catalyst was used. The design and synthesis of this new photocatalyst, [Ir(dF(CF₃ )ppy)₂ (dNMe₃ bpy)]Cl₃ , is presented. In contrast to commonly used iridium photocatalysts, this comple

SUBMITTER: van Lier RCW 

PROVIDER: S-EPMC7898865 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature