ArticleCommunications biology2022
First direct evidence for direct cell-membrane penetrations of polycationic homopoly(amino acid)s produced by bacteria.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Amphiphilic Lipid-Polymer Triblock Architectures as Nanocarriers for Therapeutic Delivery.ACS omega · 2026Article
- Live-Cell Raman Imaging Elucidates Intracellular Distribution of Macrocyclic Peptides Designed as HIV Protease Inhibitors.Chemical & biomedical imaging · 2026Article
- History of the streptothricin antibiotics and evidence for the neglect of the streptothricin resistome.npj antimicrobials and resistance · 2024Review
- Separation of an ε-poly-L-lysine derivative by solvent extraction under a controlled interfacial potential difference.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Constitutive and high gene expression in the diaminopimelate pathway accelerates ε-poly-L-lysine production in Streptomyces albulus.The Journal of antibiotics · 2023Article
- Engineering Streptomyces albulus to enhance ε-poly-L-lysine production by introducing a polyphosphate kinase-mediated ATP regeneration system.Microbial cell factories · 2023Article
- Characterization of PGuaMolecular pharmaceutics · 2023Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria produce polycationic homopoly(amino acid)s, which are characterized by isopeptide backbones. Although the biological significance of polycationic homopoly(amino acid)s remains unclear, increasing attention has recently been focused on their potential use to achieve cellular internalization. Here, for the first time, we provide direct evidence that two representative bacterial polycationic isopeptides, ε-poly-L-α-lysine (ε-PαL) and ε-oligo-L-β-lysine (ε-OβL), were internalized into mammalian cells by direct cell-membrane penetration and then diffused throughout the cytosol. In this study, we used clickable ε-PαL and ε-OβL derivatives carrying a C-terminal azide group, which were enzymatically produced and then conjugated with a fluorescent dye to analyze subcellular localization. Interestingly, fluorescent proteins conjugated with the clickable ε-PαL or ε-OβL were also internalized into cells and diffused throughout the cytosol. Notably, a Cre recombinase conjugate with ε-PαL entered cells and mediated the Cre/loxP recombination, and ε-PαL was found to deliver a full-length IgG antibody to the cytosol and nucleus.
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Registered trials
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