ArticleNucleic acids research2003
Cellular uptake of Antennapedia Penetratin peptides is a two-step process in which phase transfer precedes a tryptophan-dependent translocation.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.
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Who cites it
40 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.
- Of travelling homeoproteins and medulloblastomas.Oncogene · 2025Pooled it
- Penetratin an Old Player in the Field of Cell-Penetrating Peptides Is in New Custom-Effect of Aromatic Non-Natural Amino Acid Substitutions.Pharmaceutics · 2026Article
- Enhancing diabetes treatment by targeted nucleic acid and drug delivery using cell-penetrating peptides, peptide nucleic acids, and receptor targeting.Frontiers in pharmacology · 2026Review
- ANGEL2 Modulates Wild-type TP53 Translation and Doxorubicin Chemosensitivity in Colon Cancer.Molecular cancer research : MCR · 2025Article
- Design of Natterins-based peptides improves antimicrobial and antiviral activities.Biotechnology reports (Amsterdam, Netherlands) · 2025Article
- Transgenic tomato strategies targeting whitefly eggs from apoplastic or ovary-directed proteins.BMC plant biology · 2024Article
- Blood pressure reduction through brain delivery of nanoparticles loaded with plasmid DNA encoding angiotensin receptor shRNA.Molecular therapy. Nucleic acids · 2024Article
- Influence of Aza-Glycine Substitution on the Internalization of Penetratin.Pharmaceutics · 2024Article
- Molecular Dynamics Simulations of Drug-Conjugated Cell-Penetrating Peptides.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Protein transduction domain of translationally controlled tumor protein: characterization and application in drug delivery.Drug delivery · 2022Review
- Tuning Electrostatic and Hydrophobic Surfaces of Aromatic Rings to Enhance Membrane Association and Cell Uptake of Peptides.Angewandte Chemie (International ed. in English) · 2022Article
- Optimization of eIF4E-Binding Peptide Pep8 to Disrupt the RBM38-eIF4E Complex for Induction of p53 and Tumor Suppression.Frontiers in oncology · 2022Article
- Selective N-Arylation of p-Aminophenylalanine in Unprotected Peptides with Organometallic Palladium Reagents.Angewandte Chemie (International ed. in English) · 2021Article
- CPPs to the Test: Effects on Binding, Uptake and Biodistribution of a Tumor Targeting Nanobody.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Survivin Expression Is Differentially Regulated by a Selective Cross-talk between RBM38 and miRNAs let-7b or miR-203a.Cancer research · 2021Article
- A Global Review on Short Peptides: Frontiers and Perspectives.Molecules (Basel, Switzerland) · 2021Review
- In Vitro and Ex Vivo Evaluation of Penetratin as a Non-invasive Permeation Enhancer in the Penetration of Salmon Calcitonin through TR146 Buccal Cells and Porcine Buccal Tissues.Pharmaceuticals (Basel, Switzerland) · 2020Article
- Disruption of the Rbm38-eIF4E Complex with a Synthetic Peptide Pep8 Increases p53 Expression.Cancer research · 2019Article
- Mechanisms of Cellular Internalization of Quantum Dot® Conjugated Bone Formation Mimetic Peptide CK2.3.Nanomaterials (Basel, Switzerland) · 2018Article
- Increased Expression of Transcription Factor SRY-box-Containing Gene 11 (Sox11) Enhances Neurite Growth by Regulating Neurotrophic Factor Responsiveness.Neuroscience · 2018Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several homeodomains and homeodomain-containing proteins enter live cells through a receptor- and energy-independent mechanism. Translocation through biological membranes is conferred by the third alpha-helix of the homeodomain, also known as Penetratin. Biophysical studies demonstrate that entry of Penetratin into cells requires its binding to surface lipids but that binding and translocation are differentially affected by modifications of some physico-chemical properties of the peptide, like helical amphipathicity or net charge. This suggests that the plasma membrane lipid composition affects the internalization of Penetratin and that internalization requires both lipid binding and other specific properties. Using a phase transfer assay, it is shown that negatively charged lipids promote the transfer of Penetratin from a hydrophilic into a hydrophobic environment, probably through charge neutralization. Accordingly, transfer into a hydrophobic milieu can also be obtained in the absence of negatively charged lipids, by the addition of DNA oligonucleotides. Strikingly, phase transfer by charge neutralization was also observed with a variant peptide of same charge and hydrophobicity in which the tryptophan at position 6 was replaced by a phenylalanine. However, Penetratin, but not its mutant version, is internalized by live cells. This underscores that charge neutralization and phase transfer represent only a first step in the internalization process and that further crossing of a biological membrane necessitates the critical tryptophan residue at position 6.
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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.