Using LanM Enzymes to Modify Glucagon-Like Peptides 1 and 2 in E.coli.
Chembiochem
; 25(13): e202400201, 2024 Jul 02.
Article
in En
| MEDLINE
| ID: mdl-38701360
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 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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Escherichia coli
/
Glucagon-Like Peptide 1
/
Glucagon-Like Peptide 2
Language:
En
Journal:
Chembiochem
Journal subject:
BIOQUIMICA
Year:
2024
Document type:
Article
Affiliation country:
Denmark
Country of publication:
Germany