ArticleChembiochem : a European journal of chemical biology2019
Bioorthogonal Metalloporphyrin-Catalyzed Selective Methionine Alkylation in the Lanthipeptide Nisin.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Functional Nucleic-Acid-Decorated Spherical Nanoparticles: Preparation Strategies and Current Applications in Cancer Therapy.Small science · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Combating Antimicrobial Resistance With New-To-Nature Lanthipeptides Created by Genetic Code Expansion.Frontiers in microbiology · 2020Review
- Bioorthogonal Metalloporphyrin-Catalyzed Selective Methionine Alkylation in the Lanthipeptide Nisin.Chembiochem : a European journal of chemical biology · 2019Article
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2 authors at 1 institution in 1 country.
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Abstract
Bioorthogonal catalytic modification of ribosomally synthesized and post-translationally modified peptides (RiPPs) is a promising approach to obtaining novel antimicrobial peptides with improved properties and/or activities. Here, we present the serendipitous discovery of a selective and rapid method for the alkylation of methionines in the lanthipeptide nisin. Using carbenes, formed from water-soluble metalloporphyrins and diazoacetates, methionines are alkylated to obtain sulfonium ions. The formed sulfonium ions are stable, but can be further reacted to obtain functionalized methionine analogues, expanding the toolbox of chemical posttranslational modification even further.
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