Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-11020
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Main Title: Conjugation of Synthetic Polyproline Moietes to Lipid II Binding Fragments of Nisin Yields Active and Stable Antimicrobials
Author(s): Deng, Jingjing
Viel, Jakob H.
Kubyshkin, Vladimir
Budisa, Nediljko
Kuipers, Oscar P.
Type: Article
Language Code: en
Abstract: Coupling functional moieties to lantibiotics offers exciting opportunities to produce novel derivatives with desirable properties enabling new functions and applications. Here, five different synthetic hydrophobic polyproline peptides were conjugated to either nisin AB (the first two rings of nisin) or nisin ABC (the first three rings of nisin) by using click chemistry. The antimicrobial activity of nisin ABC + O6K3 against Enterococcus faecium decreased 8-fold compared to full-length nisin, but its activity was 16-fold better than nisin ABC, suggesting that modifying nisin ABC is a promising strategy to generate semi-synthetic nisin hybrids. In addition, the resulting nisin hybrids are not prone to degradation at the C-terminus, which has been observed for nisin as it can be degraded by nisinase or other proteolytic enzymes. This methodology allows for getting more insight into the possibility of creating semi-synthetic nisin hybrids that maintain antimicrobial activity, in particular when synthetic and non-proteinaceous moieties are used. The success of this approach in creating viable nisin hybrids encourages further exploring the use of different modules, e.g., glycans, lipids, active peptide moieties, and other antimicrobial moieties.
URI: https://depositonce.tu-berlin.de/handle/11303/12146
http://dx.doi.org/10.14279/depositonce-11020
Issue Date: 20-Nov-2020
Date Available: 8-Dec-2020
DDC Class: 570 Biowissenschaften; Biologie
Subject(s): click chemistry
RiPPs
lantibiotics
nisin
polyproline peptides
License: https://creativecommons.org/licenses/by/4.0/
Journal Title: Frontiers in Microbiology
Publisher: Frontiers
Publisher Place: Lausanne
Volume: 11
Article Number: 575334
Publisher DOI: 10.3389/fmicb.2020.575334
EISSN: 1664-302X
Appears in Collections:FG Biokatalyse » Publications

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