Pyrrole-Mediated Peptide Cyclization Identified through Genetically Reprogrammed Peptide Synthesis.

ABSTRACT: Flexible in vitro translation (FIT) was used as a screening method to uncover a new methodology for peptide constraining based on the attack of a nucleophilic side-chain functionality onto an oxidized furylalanine side chain. A set of template peptides, each containing furylalanine as furan-modified amino acid and a nucleophilic residue (Cys, His, Lys, Arg, Ser, or Tyr), was produced through FIT. The translation mixtures were treated with N-bromosuccinimide (NBS) to achieve selective furan oxidation and subsequent MALDI analysis demonstrated Lys and Ser as promising residues for cyclisation. Solid-phase peptide synthesis (SPPS) was used to synthesize suitable amounts of material for further in-depth analysis and characterisation. It was found that in the case of the peptide containi

SUBMITTER: Decoene KW 

PROVIDER: S-EPMC6315747 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature