ArticleProceedings of the National Academy of Sciences of the United States of America2017
Self-association of a highly charged arginine-rich cell-penetrating peptide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Multi-Site Aggregation of p53: Insights from Self- and Co-Aggregation of Multiple Aggregation-Prone Regions.ACS omega · 2026Article
- HyRes: Accurate Physics-Based Simulation of Dynamic Protein Structures and Interactions in Complex Environments at Scale.bioRxiv : the preprint server for biology · 2026Article
- Deciphering the Influence of Side Chains of Short Cationic Hydrophobic Peptides on Macroscopic and Molecular Properties of Mixed Lipid Bilayers.The Journal of membrane biology · 2026Article
- Molecular Simulations of Polymer-based Drug Nanocarriers: From Physical and Structural Properties to Controlled Release.Advanced healthcare materials · 2026Review
- Very Stable High-Molecular-Mass Multiprotein Complexes in Different Organs of the Sea CucumberMolecules (Basel, Switzerland) · 2025Article
- Prediction of phase-separation propensities of disordered proteins from sequence.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Nanoparticles with Cell-Penetrating Peptides for Oral Delivery: A Case for Oral Delivery of Insulin.International journal of nanomedicine · 2025Review
- Making Proteins with Electricity.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Molecular dynamics simulations unveil the aggregation patterns and salting out of polyarginines at zwitterionic POPC bilayers in solutions of various ionic strengths.Computational and structural biotechnology journal · 2024Article
- In silico and physico-chemical characterization of cluster formation dynamics in peptide solutions.Biochemistry and biophysics reports · 2024Article
- Anion Binding to Ammonium and Guanidinium Hosts: Implications for the Reverse Hofmeister Effects Induced by Lysine and Arginine Residues.The Journal of organic chemistry · 2024Article
- Redox-responsive peptide-based complex coacervates as delivery vehicles with controlled release of proteinous drugs.Communications chemistry · 2023Article
- Cell-Surface-Retained Peptide Additives for the Cytosolic Delivery of Functional Proteins.Journal of the American Chemical Society · 2023Article
- Comprehensive Regulation of Liquid-Liquid Phase Separation of Polypeptides.Molecules (Basel, Switzerland) · 2023Article
- Adsorption/Desorption of Cationic-Hydrophobic Peptides on Zwitterionic Lipid Bilayer Is Associated with the Possibility of Proton Transfer.Antibiotics (Basel, Switzerland) · 2023Article
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- A Molecular Mechanism to Explain the Nickel-Induced Changes in Protamine-like Proteins and Their DNA Binding Affecting Sperm Chromatin inBiomolecules · 2023Article
- Translocation of a single Arg[Formula: see text] peptide across a DOPC/DOPG(4:1) model membrane using the weighted ensemble method.Scientific reports · 2023Article
- Peptides as carriers of active ingredients: A review.Current research in food science · 2023Review
Corrections and comments
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Authors and funding
9 authors.
Funding
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Abstract
Small-angle X-ray scattering (SAXS) measurements reveal a striking difference in intermolecular interactions between two short highly charged peptides-deca-arginine (R10) and deca-lysine (K10). Comparison of SAXS curves at high and low salt concentration shows that R10 self-associates, while interactions between K10 chains are purely repulsive. The self-association of R10 is stronger at lower ionic strengths, indicating that the attraction between R10 molecules has an important electrostatic component. SAXS data are complemented by NMR measurements and potentials of mean force between the peptides, calculated by means of umbrella-sampling molecular dynamics (MD) simulations. All-atom MD simulations elucidate the origin of the R10-R10 attraction by providing structural information on the dimeric state. The last two C-terminal residues of R10 constitute an adhesive patch formed by stacking of the side chains of two arginine residues and by salt bridges formed between the like-charge ion pair and the C-terminal carboxyl groups. A statistical analysis of the Protein Data Bank reveals that this mode of interaction is a common feature in proteins.
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