ArticleChembiochem : a European journal of chemical biology2022
One-Pot Chemoenzymatic Synthesis of Microviridin Analogs Containing Functional Tags.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Native Metabolomics Unveils Suomilide Analogs with Potent Trypsin Inhibitory Activity.Journal of natural products · 2026Article
- Ensemble Sensitivity to Chemical Modifications in Free and Bound Macrocyclic Peptides.The journal of physical chemistry. B · 2026Article
- A Bifunctional Protease Cleaves the Leader Peptide in the Biosynthesis of Class I Microviridins.Chembiochem : a European journal of chemical biology · 2026Article
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Discovery, Function, and Engineering of Graspetides.Trends in chemistry · 2023Article
- One-Pot Chemoenzymatic Synthesis of Microviridin Analogs Containing Functional Tags.Chembiochem : a European journal of chemical biology · 2022Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microviridins are a prominent family of ribosomally synthesized and posttranslationally modified peptides (RiPPs) featuring characteristic lactone and lactam rings. Their unusual cage-like architecture renders them highly potent serine protease inhibitors of which individual variants specifically inhibit different types of proteases of pharmacological interest. While posttranslational modifications are key for the stability and bioactivity of RiPPs, additional attractive properties can be introduced by functional tags. To date - although highly desirable - no method has been reported to incorporate functional tags in microviridin scaffolds or the overarching class of graspetides. In this study, a chemoenzymatic in vitro platform is used to introduce functional tags in various microviridin variants yielding biotinylated, dansylated or propargylated congeners. This straightforward approach paves the way for customized protease inhibitors with built-in functionalities that can help to unravel the still elusive ecological roles and targets of this remarkable class of compounds and to foster applications based on protease inhibition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.