dc.contributor.author	Deng, Jingjing
dc.contributor.author	Viel, Jakob H.
dc.contributor.author	Kubyshkin, Vladimir
dc.contributor.author	Budisa, Nediljko
dc.contributor.author	Kuipers, Oscar P.
dc.date.accessioned	2020-12-08T14:30:45Z
dc.date.available	2020-12-08T14:30:45Z
dc.date.issued	2020-11-20
dc.date.updated	2020-12-07T10:46:01Z
dc.description.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.	en
dc.identifier.eissn	1664-302X
dc.identifier.uri	https://depositonce.tu-berlin.de/handle/11303/12146
dc.identifier.uri	http://dx.doi.org/10.14279/depositonce-11020
dc.language.iso	en	en
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	en
dc.subject.ddc	570 Biowissenschaften; Biologie	de
dc.subject.other	click chemistry	en
dc.subject.other	RiPPs	en
dc.subject.other	lantibiotics	en
dc.subject.other	nisin	en
dc.subject.other	polyproline peptides	en
dc.title	Conjugation of Synthetic Polyproline Moietes to Lipid II Binding Fragments of Nisin Yields Active and Stable Antimicrobials	en
dc.type	Article	en
dc.type.version	publishedVersion	en
dcterms.bibliographicCitation.articlenumber	575334	en
dcterms.bibliographicCitation.doi	10.3389/fmicb.2020.575334	en
dcterms.bibliographicCitation.journaltitle	Frontiers in Microbiology	en
dcterms.bibliographicCitation.originalpublishername	Frontiers	en
dcterms.bibliographicCitation.originalpublisherplace	Lausanne	en
dcterms.bibliographicCitation.volume	11	en
tub.accessrights.dnb	free	en
tub.affiliation	Fak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Biokatalyse	de
tub.affiliation.faculty	Fak. 2 Mathematik und Naturwissenschaften	de
tub.affiliation.group	FG Biokatalyse	de
tub.affiliation.institute	Inst. Chemie	de
tub.publisher.universityorinstitution	Technische Universität Berlin	en

Conjugation of Synthetic Polyproline Moietes to Lipid II Binding Fragments of Nisin Yields Active and Stable Antimicrobials

Files

Original bundle

License bundle

Collections