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Triculamin: An Unusual Lasso Peptide with Potent Antimycobacterial Activity

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Triculamin: An Unusual Lasso Peptide with Potent Antimycobacterial Activity. / Andersen, Frederikke D.; Pedersen, Katja D.; Wilkens Juhl, Dennis et al.
I: Journal of Natural Products, Bind 85, Nr. 6, 06.2022, s. 1514-1521.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Andersen FD, Pedersen KD, Wilkens Juhl D, Mygind T, Chopin P, B. Svenningsen E et al. Triculamin: An Unusual Lasso Peptide with Potent Antimycobacterial Activity. Journal of Natural Products. 2022 jun.;85(6):1514-1521. doi: 10.1021/acs.jnatprod.2c00065

Author

Andersen, Frederikke D. ; Pedersen, Katja D. ; Wilkens Juhl, Dennis et al. / Triculamin : An Unusual Lasso Peptide with Potent Antimycobacterial Activity. I: Journal of Natural Products. 2022 ; Bind 85, Nr. 6. s. 1514-1521.

Bibtex

@article{806936919f6147acaeec68dfbd12321d,
title = "Triculamin: An Unusual Lasso Peptide with Potent Antimycobacterial Activity",
abstract = "Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) produced by microorganisms. Here we show that the two natural products triculamin and alboverticillin, originally isolated in 1967 and 1958, respectively, with potent and specific activity against mycobacteria are in fact the same lasso peptide. We solved the structure using 2D NMR spectroscopy and expanded on the previously reported bioactivity. Through genome sequencing, we identify the responsible biosynthetic gene clusters, which curiously revealed that, unlike any known lasso peptides, their precursor peptides appear to have a follower instead of a leader peptide. ",
keywords = "ANANTIN, ANTAGONIST, MATURATION, NATRIURETIC-FACTOR ANF, SEQUENCE, TUBERCULOSIS, Multigene Family, Peptides/chemistry, Biological Products, Protein Processing, Post-Translational",
author = "Andersen, {Frederikke D.} and Pedersen, {Katja D.} and {Wilkens Juhl}, Dennis and Tobias Mygind and Paul Chopin and {B. Svenningsen}, Esben and Poulsen, {Thomas B.} and {Braad Lund}, Marie and Andreas Schramm and Gotfredsen, {Charlotte H.} and Thomas T{\o}rring",
note = "Publisher Copyright: {\textcopyright} 2022 American Chemical Society and American Society of Pharmacognosy.",
year = "2022",
month = jun,
doi = "10.1021/acs.jnatprod.2c00065",
language = "English",
volume = "85",
pages = "1514--1521",
journal = "Journal of Natural Products",
issn = "0163-3864",
publisher = "AMER CHEMICAL SOC",
number = "6",

}

RIS

TY - JOUR

T1 - Triculamin

T2 - An Unusual Lasso Peptide with Potent Antimycobacterial Activity

AU - Andersen, Frederikke D.

AU - Pedersen, Katja D.

AU - Wilkens Juhl, Dennis

AU - Mygind, Tobias

AU - Chopin, Paul

AU - B. Svenningsen, Esben

AU - Poulsen, Thomas B.

AU - Braad Lund, Marie

AU - Schramm, Andreas

AU - Gotfredsen, Charlotte H.

AU - Tørring, Thomas

N1 - Publisher Copyright: © 2022 American Chemical Society and American Society of Pharmacognosy.

PY - 2022/6

Y1 - 2022/6

N2 - Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) produced by microorganisms. Here we show that the two natural products triculamin and alboverticillin, originally isolated in 1967 and 1958, respectively, with potent and specific activity against mycobacteria are in fact the same lasso peptide. We solved the structure using 2D NMR spectroscopy and expanded on the previously reported bioactivity. Through genome sequencing, we identify the responsible biosynthetic gene clusters, which curiously revealed that, unlike any known lasso peptides, their precursor peptides appear to have a follower instead of a leader peptide.

AB - Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) produced by microorganisms. Here we show that the two natural products triculamin and alboverticillin, originally isolated in 1967 and 1958, respectively, with potent and specific activity against mycobacteria are in fact the same lasso peptide. We solved the structure using 2D NMR spectroscopy and expanded on the previously reported bioactivity. Through genome sequencing, we identify the responsible biosynthetic gene clusters, which curiously revealed that, unlike any known lasso peptides, their precursor peptides appear to have a follower instead of a leader peptide.

KW - ANANTIN

KW - ANTAGONIST

KW - MATURATION

KW - NATRIURETIC-FACTOR ANF

KW - SEQUENCE

KW - TUBERCULOSIS

KW - Multigene Family

KW - Peptides/chemistry

KW - Biological Products

KW - Protein Processing, Post-Translational

UR - http://www.scopus.com/inward/record.url?scp=85132940390&partnerID=8YFLogxK

U2 - 10.1021/acs.jnatprod.2c00065

DO - 10.1021/acs.jnatprod.2c00065

M3 - Journal article

C2 - 35748039

AN - SCOPUS:85132940390

VL - 85

SP - 1514

EP - 1521

JO - Journal of Natural Products

JF - Journal of Natural Products

SN - 0163-3864

IS - 6

ER -