ArticleBiophysical journal2008
Binding and clustering of glycosaminoglycans: a common property of mono- and multivalent cell-penetrating compounds.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 121 citations in OpenAlex.
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- Peptide-Based Nanoparticles for Systemic Extrahepatic Delivery of Therapeutic Nucleotides.International journal of molecular sciences · 2023Review
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- Semaphorin 3A-Glycosaminoglycans Interaction as Therapeutic Target for Axonal Regeneration.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Contribution of syndecans to cellular uptake and fibrillation of α-synuclein and tau.Scientific reports · 2019Article
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- Identification of a Peptide for Systemic Brain Delivery of a Morpholino Oligonucleotide in Mouse Models of Spinal Muscular Atrophy.Nucleic acid therapeutics · 2017Article
- Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Quantitative fluorescence spectroscopy and flow cytometry analyses of cell-penetrating peptides internalization pathways: optimization, pitfalls, comparison with mass spectrometry quantification.Scientific reports · 2016Article
- Applications and Challenges for Use of Cell-Penetrating Peptides as Delivery Vectors for Peptide and Protein Cargos.International journal of molecular sciences · 2016Review
- Design and characterization of a new peptide vector for short interfering RNA delivery.Journal of nanobiotechnology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent observations in cell culture provide evidence that negatively charged glycosaminoglycans (GAGs) at the surface of biological cells bind cationic cell-penetrating compounds (CPCs) and cluster during CPC binding, thereby contributing to their endocytotic uptake. The GAG binding and clustering occur in the low-micromolar concentration range and suggest a tight interaction between GAGs and CPCs, although the relation between binding affinity and specificity of this interaction remains to be investigated. We therefore measured the GAG binding and clustering of various mono- and multivalent CPCs such as DNA transfection vectors (polyethylenimine; 1,2-dioleoyl-3-trimethylammonium-propane), amino acid homopolymers (oligoarginine; oligolysine), and cell-penetrating peptides (Penetratin; HIV-1 Tat) by means of isothermal titration calorimetry and dynamic light scattering. We find that these structurally diverse CPCs share the property of GAG binding and clustering. The binding is very tight (microscopic dissociation constants between 0.34 and 1.34 microM) and thus biologically relevant. The hydrodynamic radius of the resulting aggregates ranges from 78 nm to 586 nm, suggesting that they consist of numerous GAG chains cross-linked by CPCs. Likewise, the membrane-permeant monovalent cation acridine orange leads to GAG binding and clustering, in contrast to its membrane-impermeant structural analogs propidium iodide and ethidium bromide. Because the binding and clustering of GAGs were found to be a common denominator of all CPCs tested, these properties might be helpful to identify further CPCs.
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Registered trials
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