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

Autor: Larsen CK; Department of Biological and Chemical Engineering, Aarhus University, 8000, Aarhus C, Denmark.; Novo Nordisk A/S, 2760, Måløv, Denmark., Lindquist P; Department of Biomedical Sciences, University of Copenhagen, 2100, Copenhagen, Denmark., Rosenkilde M; Department of Biomedical Sciences, University of Copenhagen, 2100, Copenhagen, Denmark., Madsen AR; Novo Nordisk A/S, 2760, Måløv, Denmark., Haselmann K; Novo Nordisk A/S, 2760, Måløv, Denmark., Glendorf T; Novo Nordisk A/S, 2760, Måløv, Denmark., Olesen K; Novo Nordisk A/S, 2760, Måløv, Denmark., Kodal ALB; Novo Nordisk A/S, 2760, Måløv, Denmark., Tørring T; Department of Biological and Chemical Engineering, Aarhus University, 8000, Aarhus C, Denmark.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Jul 02; Vol. 25 (13), pp. e202400201. Date of Electronic Publication: 2024 Jun 14.
DOI: 10.1002/cbic.202400201
Abstrakt: 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.
(© 2024 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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