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- W4328114259 abstract "Abstract 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 removed as the last step of biosynthesis. Here, we exploit leader peptides and their matching enzymes to investigate the installment 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." @default.
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- W4328114259 date "2023-03-20" @default.
- W4328114259 modified "2023-09-27" @default.
- W4328114259 title "Using LanM Enzymes to Modify Glucagon-Like Peptides 1 and 2 in<i>E.coli</i>" @default.
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- W4328114259 doi "https://doi.org/10.1101/2023.03.20.532734" @default.
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