Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides. / Gless, Bengt H.; Bejder, Benjamin Svejdal; Monda, Fabrizio; Bojer, Martin S.; Ingmer, Hanne; Olsen, Christian A.

In: Journal of the American Chemical Society, Vol. 143, No. 28, 2021, p. 10514–10518.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gless, BH, Bejder, BS, Monda, F, Bojer, MS, Ingmer, H & Olsen, CA 2021, 'Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides', Journal of the American Chemical Society, vol. 143, no. 28, pp. 10514–10518. https://doi.org/10.1021/jacs.1c02614

APA

Gless, B. H., Bejder, B. S., Monda, F., Bojer, M. S., Ingmer, H., & Olsen, C. A. (2021). Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides. Journal of the American Chemical Society, 143(28), 10514–10518. https://doi.org/10.1021/jacs.1c02614

Vancouver

Gless BH, Bejder BS, Monda F, Bojer MS, Ingmer H, Olsen CA. Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides. Journal of the American Chemical Society. 2021;143(28):10514–10518. https://doi.org/10.1021/jacs.1c02614

Author

Gless, Bengt H. ; Bejder, Benjamin Svejdal ; Monda, Fabrizio ; Bojer, Martin S. ; Ingmer, Hanne ; Olsen, Christian A. / Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides. In: Journal of the American Chemical Society. 2021 ; Vol. 143, No. 28. pp. 10514–10518.

Bibtex

@article{84d51afee5284fc6b76b18cca30b465c,
title = "Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides",
abstract = "Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in the regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci, for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has also been predicted to constitute a structural feature of AIPs from other genera. Here, we show that pentameric AIPs from Lactiplantibacillus plantarum, Clostridium perfringens, and Listeria monocytogenes that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of cross-species and potential cross-genus communication of bacteria and may help guide the discovery of peptide ligands to perturb their function. ",
author = "Gless, {Bengt H.} and Bejder, {Benjamin Svejdal} and Fabrizio Monda and Bojer, {Martin S.} and Hanne Ingmer and Olsen, {Christian A.}",
note = "Publisher Copyright: {\textcopyright} 2021 American Chemical Society.",
year = "2021",
doi = "10.1021/jacs.1c02614",
language = "English",
volume = "143",
pages = "10514–10518",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "28",

}

RIS

TY - JOUR

T1 - Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides

AU - Gless, Bengt H.

AU - Bejder, Benjamin Svejdal

AU - Monda, Fabrizio

AU - Bojer, Martin S.

AU - Ingmer, Hanne

AU - Olsen, Christian A.

N1 - Publisher Copyright: © 2021 American Chemical Society.

PY - 2021

Y1 - 2021

N2 - Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in the regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci, for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has also been predicted to constitute a structural feature of AIPs from other genera. Here, we show that pentameric AIPs from Lactiplantibacillus plantarum, Clostridium perfringens, and Listeria monocytogenes that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of cross-species and potential cross-genus communication of bacteria and may help guide the discovery of peptide ligands to perturb their function.

AB - Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in the regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci, for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has also been predicted to constitute a structural feature of AIPs from other genera. Here, we show that pentameric AIPs from Lactiplantibacillus plantarum, Clostridium perfringens, and Listeria monocytogenes that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of cross-species and potential cross-genus communication of bacteria and may help guide the discovery of peptide ligands to perturb their function.

U2 - 10.1021/jacs.1c02614

DO - 10.1021/jacs.1c02614

M3 - Journal article

C2 - 34228933

AN - SCOPUS:85110987964

VL - 143

SP - 10514

EP - 10518

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 28

ER -

ID: 275827995