ArticleACS synthetic biology2021
Semisynthetic Macrocyclic Lipo-lanthipeptides Display Antimicrobial Activity Against Bacterial Pathogens.
Article in ACS synthetic biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Biosynthesis of Antimicrobial Ornithine-Containing Lacticin 481 Analogues by Use of a Combinatorial Biosynthetic Pathway inACS synthetic biology · 2024Article
- A review of current antibiotic resistance and promising antibiotics with novel modes of action to combat antibiotic resistance.Archives of microbiology · 2023Review
- Lipidated variants of the antimicrobial peptide nisin produced via incorporation of methionine analogs for click chemistry show improved bioactivity.The Journal of biological chemistry · 2023Article
- Genome sequencing and analysis ofFrontiers in microbiology · 2023Article
- Brevicidine acts as an effective sensitizer of outer membrane-impermeable conventional antibiotics forFrontiers in microbiology · 2023Article
- Striving for sustainable biosynthesis: discovery, diversification, and production of antimicrobial drugs in Escherichia coli.Biochemical Society transactions · 2022Review
- Modular Use of the Uniquely Small Ring A of Mersacidin Generates the Smallest Ribosomally Produced Lanthipeptide.ACS synthetic biology · 2022Article
- Mutational Studies of the Mersacidin Leader Reveal the Function of Its Unique Two-Step Leader Processing Mechanism.ACS synthetic biology · 2022Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A large number of antimicrobial peptides depend on intramolecular disulfide bonds for their biological activity. However, the relative instability of disulfide bonds has limited the potential of some of these peptides to be developed into therapeutics. Conversely, peptides containing intramolecular (methyl)lanthionine-based bonds, lanthipeptides, are highly stable under a broader range of biological and physical conditions. Here, the class-II lanthipeptide synthetase CinM, from the cinnamycin gene cluster, was employed to create methyllanthionine stabilized analogues of disulfide-bond-containing antimicrobial peptides. The resulting analogues were subsequently modified
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