ArticleMolecular biotechnology2016
Effect of a Flexible Linker on Recombinant Expression of Cell-Penetrating Peptide Fusion Proteins and Their Translocation into Fungal Cells.
Article in Molecular biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Metabolic engineeringSynthetic and systems biotechnology · 2025Article
- Sneaking in SpyCatcher using cell penetrating peptides forNanotechnology · 2023Article
- First direct evidence for direct cell-membrane penetrations of polycationic homopoly(amino acid)s produced by bacteria.Communications biology · 2022Article
- Cell-penetrating peptide for targeted macromolecule delivery into plant chloroplasts.Applied microbiology and biotechnology · 2022Article
- TAQing2.0 for genome reorganization of asexual industrial yeasts by direct protein transfection.Communications biology · 2022Article
- Cupid, a cell permeable peptide derived from amoeba, capable of delivering GFP into a diverse range of species.Scientific reports · 2020Article
- Effect of linkers on immobilization of scFvs with biotin-streptavidin interaction.Biotechnology and applied biochemistry · 2018Article
- Secondary structure of cell-penetrating peptides during interaction with fungal cells.Protein science : a publication of the Protein Society · 2018Article
- Fusion proteins towards fungi and bacteria in plant protection.Microbiology (Reading, England) · 2018Article
- Translocation of cell-penetrating peptides into Candida fungal pathogens.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell-penetrating peptides (CPPs) are a class of small peptides that are able to cross cell membranes via direct translocation or endocytosis. They have been widely used to deliver tethered bioactive molecules to cells, but recombinantly producing CPPs as fusions to protein cargo leads to low yields. We used Escherichia coli cells to recombinantly produce genetic fusions of NPFSD (derived from a yeast endocytosis signal) and pVEC (derived from a murine vascular endothelium cadherin) to the N-terminus of green fluorescent protein (GFP) with and without a flexible glycine-serine linker between the CPP and GFP. The flexible linker improved the expression of the NPFSD construct and the pVEC construct, resulting in a 24.5 % improvement in yield for the NPFSD fusion and a 50.0 % improvement in yield for the pVEC fusion. The linker did not diminish the ability of the fusions to translocate into the fungal pathogen Candida albicans, and the translocation of the NPFSD constructs actually increased by 58 % at 10 min. Moreover, the toxicity of the fusions towards C. albicans was not affected by the incorporation of the linker. These results illustrate the utility of including a linker for CPP-cargo fusions and the potential of NPFSD and pVEC fusions for use in delivering protein cargo to C. albicans.
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