ArticleNature communications2017
Phage display and selection of lanthipeptides on the carboxy-terminus of the gene-3 minor coat protein.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers, 1 of them a synthesis that pooled it.
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Who cites it
64 citing papers in PubMed, 1 synthesis or guideline pooled it, 114 citations in OpenAlex.
- Advancements in the Application of Ribosomally Synthesized and Post-Translationally Modified Peptides (RiPPs).Biomolecules · 2024Pooled it
- Sortase-mediated generation of various macrocyclic peptide scaffolds from low-reactivity electrophilic substrates.Chemical science · 2026Article
- Affinity improvement of specific scFvs interacting with the Neisseria meningitidis factor H-binding protein: a molecular dynamics simulation approach and experimental study.BMC biotechnology · 2026Article
- Lan enzyme-free construction of lanthionine-bridged macrocyclic phage libraries.Chemical science · 2026Article
- Computational structure prediction of lanthipeptides with NMR data reveals underappreciated peptide flexibility.Protein science : a publication of the Protein Society · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Kinetic Analysis of Cyclization by the Substrate-Tolerant Lanthipeptide Synthetase ProcM.ACS catalysis · 2024Article
- Assessing the Impact of the Leader Peptide in Protease Inhibition by the Microviridin Family of RiPPs.Biomedicines · 2024Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- Expression and Subcellular Localization of Lanthipeptides in Human Cells.ACS synthetic biology · 2024Article
- Employing unnatural promiscuity of sortase to construct peptide macrocycle libraries for ligand discovery.Chemical science · 2024Article
- Use of a head-to-tail peptide cyclase to prepare hybrid RiPPs.Chemical communications (Cambridge, England) · 2024Article
- Biosynthesis of Macrocyclic Peptides with C-Terminal β-Amino-α-keto Acid Groups by Three Different Metalloenzymes.ACS central science · 2024Article
- Kinetic Analysis of Lanthipeptide Cyclization by Substrate-Tolerant ProcM.bioRxiv : the preprint server for biology · 2024Article
- Diversification of Phage-Displayed Peptide Libraries with Noncanonical Amino Acid Mutagenesis and Chemical Modification.Chemical reviews · 2024Review
- Strategies for the Construction of Multicyclic Phage Display Libraries.Chembiochem : a European journal of chemical biology · 2024Review
- Genome Mining for New Enzyme Chemistry.ACS catalysis · 2024Review
- Biocompatible strategies for peptide macrocyclisation.Chemical science · 2024Review
- Biosynthesis of macrocyclic peptides with C-terminal β-amino-α-keto acid groups by three different metalloenzymes.bioRxiv : the preprint server for biology · 2024Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are an emerging class of natural products with drug-like properties. To fully exploit the potential of RiPPs as peptide drug candidates, tools for their systematic engineering are required. Here we report the engineering of lanthipeptides, a subclass of RiPPs characterized by multiple thioether cycles that are enzymatically introduced in a regio- and stereospecific manner, by phage display. This was achieved by heterologous co-expression of linear lanthipeptide precursors fused to the widely neglected C-terminus of the bacteriophage M13 minor coat protein pIII, rather than the conventionally used N-terminus, along with the modifying enzymes from distantly related bacteria. We observe that C-terminal precursor peptide fusions to pIII are enzymatically modified in the cytoplasm of the producing cell and subsequently displayed as mature cyclic peptides on the phage surface. Biopanning of large C-terminal display libraries readily identifies artificial lanthipeptide ligands specific to urokinase plasminogen activator (uPA) and streptavidin.
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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.