Publication

Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale

Schmitt, S., Montalbán-López, M., Peterhoff, D., Deng, J., Wagner, R., Held, M., Kuipers, O. P. & Panke, S., May-2019, In : Nature Chemical Biology. 15, 5, p. 437-443 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Schmitt, S., Montalbán-López, M., Peterhoff, D., Deng, J., Wagner, R., Held, M., ... Panke, S. (2019). Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale. Nature Chemical Biology, 15(5), 437-443. https://doi.org/10.1038/s41589-019-0250-5

Author

Schmitt, Steven ; Montalbán-López, Manuel ; Peterhoff, David ; Deng, Jingjing ; Wagner, Ralf ; Held, Martin ; Kuipers, Oscar P ; Panke, Sven. / Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale. In: Nature Chemical Biology. 2019 ; Vol. 15, No. 5. pp. 437-443.

Harvard

Schmitt, S, Montalbán-López, M, Peterhoff, D, Deng, J, Wagner, R, Held, M, Kuipers, OP & Panke, S 2019, 'Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale', Nature Chemical Biology, vol. 15, no. 5, pp. 437-443. https://doi.org/10.1038/s41589-019-0250-5

Standard

Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale. / Schmitt, Steven; Montalbán-López, Manuel; Peterhoff, David; Deng, Jingjing; Wagner, Ralf; Held, Martin; Kuipers, Oscar P; Panke, Sven.

In: Nature Chemical Biology, Vol. 15, No. 5, 05.2019, p. 437-443.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Schmitt S, Montalbán-López M, Peterhoff D, Deng J, Wagner R, Held M et al. Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale. Nature Chemical Biology. 2019 May;15(5):437-443. https://doi.org/10.1038/s41589-019-0250-5


BibTeX

@article{107ad054cf034d439ad48eda6c1a257b,
title = "Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale",
abstract = "The rise of antibiotic resistance demands the acceleration of molecular diversification strategies to inspire new chemical entities for antibiotic medicines. We report here on the large-scale engineering of ribosomally synthesized and post-translationally modified antimicrobial peptides carrying the ring-forming amino acid lanthionine. New-to-nature variants featuring distinct properties were obtained by combinatorial shuffling of peptide modules derived from 12 natural antimicrobial lanthipeptides and processing by a promiscuous post-translational modification machinery. For experimental characterization, we developed the nanoFleming, a miniaturized and parallelized high-throughput inhibition assay. On the basis of a hit set of >100 molecules, we identified variants with improved activity against pathogenic bacteria and shifted activity profiles, and extrapolated design guidelines that will simplify the identification of peptide-based anti-infectives in the future.",
keywords = "NATURAL-PRODUCTS, PEPTIDE, NISIN, BIOSYNTHESIS, LANTIBIOTICS, PROTEIN, LEADER, PROMISCUITY, MACHINERY, PLATFORM",
author = "Steven Schmitt and Manuel Montalb{\'a}n-L{\'o}pez and David Peterhoff and Jingjing Deng and Ralf Wagner and Martin Held and Kuipers, {Oscar P} and Sven Panke",
year = "2019",
month = "5",
doi = "10.1038/s41589-019-0250-5",
language = "English",
volume = "15",
pages = "437--443",
journal = "Nature Chemical Biology",
issn = "1552-4469",
number = "5",

}

RIS

TY - JOUR

T1 - Analysis of modular bioengineered antimicrobial lanthipeptides at nanoliter scale

AU - Schmitt, Steven

AU - Montalbán-López, Manuel

AU - Peterhoff, David

AU - Deng, Jingjing

AU - Wagner, Ralf

AU - Held, Martin

AU - Kuipers, Oscar P

AU - Panke, Sven

PY - 2019/5

Y1 - 2019/5

N2 - The rise of antibiotic resistance demands the acceleration of molecular diversification strategies to inspire new chemical entities for antibiotic medicines. We report here on the large-scale engineering of ribosomally synthesized and post-translationally modified antimicrobial peptides carrying the ring-forming amino acid lanthionine. New-to-nature variants featuring distinct properties were obtained by combinatorial shuffling of peptide modules derived from 12 natural antimicrobial lanthipeptides and processing by a promiscuous post-translational modification machinery. For experimental characterization, we developed the nanoFleming, a miniaturized and parallelized high-throughput inhibition assay. On the basis of a hit set of >100 molecules, we identified variants with improved activity against pathogenic bacteria and shifted activity profiles, and extrapolated design guidelines that will simplify the identification of peptide-based anti-infectives in the future.

AB - The rise of antibiotic resistance demands the acceleration of molecular diversification strategies to inspire new chemical entities for antibiotic medicines. We report here on the large-scale engineering of ribosomally synthesized and post-translationally modified antimicrobial peptides carrying the ring-forming amino acid lanthionine. New-to-nature variants featuring distinct properties were obtained by combinatorial shuffling of peptide modules derived from 12 natural antimicrobial lanthipeptides and processing by a promiscuous post-translational modification machinery. For experimental characterization, we developed the nanoFleming, a miniaturized and parallelized high-throughput inhibition assay. On the basis of a hit set of >100 molecules, we identified variants with improved activity against pathogenic bacteria and shifted activity profiles, and extrapolated design guidelines that will simplify the identification of peptide-based anti-infectives in the future.

KW - NATURAL-PRODUCTS

KW - PEPTIDE

KW - NISIN

KW - BIOSYNTHESIS

KW - LANTIBIOTICS

KW - PROTEIN

KW - LEADER

KW - PROMISCUITY

KW - MACHINERY

KW - PLATFORM

U2 - 10.1038/s41589-019-0250-5

DO - 10.1038/s41589-019-0250-5

M3 - Article

C2 - 30936500

VL - 15

SP - 437

EP - 443

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4469

IS - 5

ER -

ID: 79393488