ArticleMolecular therapy : the journal of the American Society of Gene Therapy2009
Cell-surface accumulation of flock house virus-derived peptide leads to efficient internalization via macropinocytosis.
Article in Molecular therapy : the journal of the American Society of Gene Therapy, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 118 citations in OpenAlex.
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- Efficient Direct Cytosolic Protein Delivery via Protein-Linker Co-engineering.ACS applied materials & interfaces · 2025Article
- An aegerolysin-like protein from Heliothis virescens ascovirus 3h (HvAV-3h) shows immune suppression and antibacterial activity.The Journal of general virology · 2025Article
- Rottlerin inhibits macropinocytosis of Porcine Reproductive and Respiratory Syndrome Virus through the PKCδ-Cofilin signaling pathway.PloS one · 2025Article
- Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- Bioengineering extracellular vesicle cargo for optimal therapeutic efficiency.Molecular therapy. Methods & clinical development · 2024Review
- Extracellular Microvesicles Modified with Arginine-Rich Peptides for Active Macropinocytosis Induction and Delivery of Therapeutic Molecules.ACS applied materials & interfaces · 2024Article
- Nanoplatforms for the Delivery of Nucleic Acids into Plant Cells.International journal of molecular sciences · 2023Review
- Inkjet-Based Intracellular Delivery System that Effectively Utilizes Cell-Penetrating Peptides for Cytosolic Introduction of Biomacromolecules through the Cell Membrane.ACS applied materials & interfaces · 2023Article
- A Comparison of Cellular Uptake Mechanisms, Delivery Efficacy, and Intracellular Fate between Liposomes and Extracellular Vesicles.Advanced healthcare materials · 2023Review
- In vivo direct cell-penetrating peptide mediated protein transduction system in Acyrthosiphon pisum.BMC research notes · 2023Article
- The Chemical Inhibitors of Endocytosis: From Mechanisms to Potential Clinical Applications.Cells · 2023Review
- Cell-Penetrating Peptides as Valuable Tools for Nose-to-Brain Delivery of Biological Drugs.Cells · 2023Review
- Light-Induced Condensation of Biofunctional Molecules around Targeted Living Cells to Accelerate Cytosolic Delivery.Nano letters · 2022Article
- Structure-Uptake Relationship Study of DABCYL Derivatives Linked to Cyclic Cell-Penetrating Peptides for Live-Cell Delivery of Synthetic Proteins.Angewandte Chemie (International ed. in English) · 2022Article
- GAPDH controls extracellular vesicle biogenesis and enhances the therapeutic potential of EV mediated siRNA delivery to the brain.Nature communications · 2021Article
- Phosphorescent Ir(III) complexes conjugated with oligoarginine peptides serve as optical probes for in vivo microvascular imaging.Scientific reports · 2021Article
- Decoding the proteome of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) for cell-penetrating peptides involved in pathogenesis or applicable as drug delivery vectors.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2020Article
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7 authors at 2 institutions in 1 country.
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Abstract
Arginine-rich cell-penetrating peptides (CPPs), including human immunodeficiency virus type 1 (HIV-1) Tat (48-60) and oligoarginines, have been applied as carriers for delivery of cargo molecules, because of their capacity to internalize into cells and penetrate biological membranes. Despite the fact that they have been extensively studied, the factors required for the efficient internalization of CPPs are still unclear. In this report, we evaluated the internalization efficiencies of seven CPPs derived from DNA/RNA-binding peptides, and discovered that a peptide derived from the flock house virus (FHV) coat protein was internalized most efficiently into Chinese hamster ovary (CHO-K1), HeLa, and Jurkat cells. Comparison of the factors facilitating the internalization with those of the Tat peptide revealed that the FHV peptide induces macropinocytosis much more efficiently than the Tat peptide, which leads to its high cellular uptake efficiency. Additionally, the strong adsorption of the FHV peptide on cell membranes via glycosaminoglycans (GAGs) was shown to be a key factor for induction of macropinocytosis, and these steps were successfully monitored by live imaging of the peptide internalization into cells in relation to the actin organization. The remarkable methods of FHV peptide internalization thus highlighted the critical factors for internalizations of the arginine-rich CPPs.
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