ArticleCatalysts (Basel, Switzerland)2020
Indole C6 Functionalization of Tryprostatin B Using Prenyltransferase CdpNPT.
Article in Catalysts (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Chemoenzymatic Modification of Daptomycin: Aromatic Group Installation on Trp1.Chembiochem : a European journal of chemical biology · 2024Article
- Molecular authentication, metabolite profiling and in silico-in vitro cytotoxicity screening of endophytic3 Biotech · 2024Article
- Unlocking New Prenylation Modes: Azaindoles as a New Substrate Class for Indole Prenyltransferases.ChemCatChem · 2023Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Chemoenzymatic Late-Stage Modifications Enable Downstream Click-Mediated Fluorescent Tagging of Peptides.Angewandte Chemie (International ed. in English) · 2023Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Tryprostatin A and B are prenylated, tryptophan-containing, diketopiperazine natural products, displaying cytotoxic activity through different mechanisms of action. The presence of the 6-methoxy substituent on the indole moiety of tryprostatin A was shown to be essential for the dual inhibition of topoisomerase II and tubulin polymerization. However, the inability to perform late-stage modification of the indole ring has limited the structure-activity relationship studies of this class of natural products. Herein, we describe an efficient chemoenzymatic approach for the late-stage modification of tryprostatin B using a cyclic dipeptide
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