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

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Standard

Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli. / Kjeldgaard Larsen, Camilla; Lindquist, Peter; Rosenkilde, Mette; Ravn Madsen, Alice; Haselmann, Kim; Glendorf, Tine; Olesen, Kjeld; Bank Kodal, Anne Louise; Tørring, Thomas.

I: ChemBioChem, 03.05.2024, s. e202400201.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Kjeldgaard Larsen, C, Lindquist, P, Rosenkilde, M, Ravn Madsen, A, Haselmann, K, Glendorf, T, Olesen, K, Bank Kodal, AL & Tørring, T 2024, 'Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli', ChemBioChem, s. e202400201. https://doi.org/10.1002/cbic.202400201

APA

Kjeldgaard Larsen, C., Lindquist, P., Rosenkilde, M., Ravn Madsen, A., Haselmann, K., Glendorf, T., Olesen, K., Bank Kodal, A. L., & Tørring, T. (2024). Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli. ChemBioChem, e202400201. https://doi.org/10.1002/cbic.202400201

Vancouver

Kjeldgaard Larsen C, Lindquist P, Rosenkilde M, Ravn Madsen A, Haselmann K, Glendorf T o.a. Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli. ChemBioChem. 2024 maj 3;e202400201. https://doi.org/10.1002/cbic.202400201

Author

Kjeldgaard Larsen, Camilla ; Lindquist, Peter ; Rosenkilde, Mette ; Ravn Madsen, Alice ; Haselmann, Kim ; Glendorf, Tine ; Olesen, Kjeld ; Bank Kodal, Anne Louise ; Tørring, Thomas. / Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli. I: ChemBioChem. 2024 ; s. e202400201.

Bibtex

@article{755ab0d4e0d644d7bb2209d27aa84177,

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

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.",

author = "{Kjeldgaard Larsen}, Camilla and Peter Lindquist and Mette Rosenkilde and {Ravn Madsen}, Alice and Kim Haselmann and Tine Glendorf and Kjeld Olesen and {Bank Kodal}, {Anne Louise} and Thomas T{\o}rring",

note = "{\textcopyright} 2024 Wiley‐VCH GmbH.",

year = "2024",

month = may,

day = "3",

doi = "10.1002/cbic.202400201",

language = "English",

pages = "e202400201",

journal = "ChemBioChem",

issn = "1439-4227",

publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",

}

RIS

TY - JOUR

T1 - Using LanM Enzymes to Modify Glycagon-Like Peptides 1 and 2 in E.coli

AU - Kjeldgaard Larsen, Camilla

AU - Lindquist, Peter

AU - Rosenkilde, Mette

AU - Ravn Madsen, Alice

AU - Haselmann, Kim

AU - Glendorf, Tine

AU - Olesen, Kjeld

AU - Bank Kodal, Anne Louise

AU - Tørring, Thomas

PY - 2024/5/3

Y1 - 2024/5/3

N2 - 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.

AB - 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.

U2 - 10.1002/cbic.202400201

DO - 10.1002/cbic.202400201

M3 - Journal article

C2 - 38701360

SP - e202400201

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

ER -

ID: 390885096

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