Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli

Research output: Contribution to journalJournal articleResearchpeer-review

Selective modification of peptides is often exploited to improve pharmaceutically relevant properties of bioactive peptides like stability, circulation time, and potency. In Nature, natural products belonging to the class of ribosomally synthesized and post-translationally modified peptides (RiPPs) are known to install a number of highly attractive modifications with high selectivity. These modifications are installed by enzymes guided to the peptide by corresponding leader peptides that are removed as the last step of biosynthesis. Here, we exploit leader peptides and their matching enzymes to investigate the installation of D-Ala post-translationally in a critical position in the hormones, glucagon-like peptides (GLP) 1 and 2. We also offer insight into how precursor peptide design can modulate the modification pattern achieved.

Original languageEnglish
Pages (from-to)e202400201
Publication statusE-pub ahead of print - 3 May 2024

Bibliographical note

© 2024 Wiley‐VCH GmbH.

ID: 390885096