ArticleJournal of the American Chemical Society2014
Fundamental molecular mechanism for the cellular uptake of guanidinium-rich molecules.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
80 citing papers in PubMed, 240 citations in OpenAlex.
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- Edge-Grafted Polyarginine Functionalization of Graphene Nanocarriers Maintains Noncovalent Aromatic Drug Loading.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
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- L-Arginine as an Adjuvant Chemosensitizer: Enhancement of Intestinal Permeability and Cytotoxic Activity of Doxorubicin.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Nanomolar Affinity Host-Dye Reporter Pairs from Fluorescently Labeled Oligoarginine Peptides and p-Sulfonatocalix[4]arene.Chembiochem : a European journal of chemical biology · 2026Article
- Design and biological evaluation of peptide disruptors targeting YAP1-TEAD interaction for oral cancer.BMC oral health · 2025Article
- Ionizable guanidine-based lipid nanoparticle for targeted mRNA delivery and cancer immunotherapy.Science advances · 2025Article
- Influence of lactulose as a composition of organic-mineral feed additive on broiler chicken productivity, feed digestibility, and microbiome.Veterinary world · 2025Article
- Biological Properties of Arginine-rich Peptides and their Application in Cargo Delivery to Cancer.Current drug delivery · 2025Review
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- Cell-penetrating peptides TAT and 8R functionalize P22 virus-like particles to enhance tissue distribution and retentionFrontiers in veterinary science · 2024Article
- Antimicrobial-loaded biodegradable nanoemulsions for efficient clearance of intracellular pathogens in bacterial peritonitis.Biomaterials · 2023Article
- Molecular Dynamics Simulations of Drug-Conjugated Cell-Penetrating Peptides.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Recent Progress of Rational Modified Nanocarriers for Cytosolic Protein Delivery.Pharmaceutics · 2023Review
- Enhancing the Effectiveness of Oligonucleotide Therapeutics Using Cell-Penetrating Peptide Conjugation, Chemical Modification, and Carrier-Based Delivery Strategies.Pharmaceutics · 2023Review
- Review
20 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Guanidinium-rich molecules, such as cell-penetrating peptides, efficiently enter living cells in a non-endocytic energy-independent manner and transport a wide range of cargos, including drugs and biomarkers. The mechanism by which these highly cationic molecules efficiently cross the hydrophobic barrier imposed by the plasma membrane remains a fundamental open question. Here, a combination of computational results and in vitro and live-cell experimental evidence reveals an efficient energy-independent translocation mechanism for arginine-rich molecules. This mechanism unveils the essential role of guanidinium groups and two universal cell components: fatty acids and the cell membrane pH gradient. Deprotonated fatty acids in contact with the cell exterior interact with guanidinium groups, leading to a transient membrane channel that facilitates the transport of arginine-rich peptides toward the cell interior. On the cytosolic side, the fatty acids become protonated, releasing the peptides and resealing the channel. This fundamental mechanism appears to be universal across cells from different species and kingdoms.
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What OpenQuestion holds
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.