ArticleBiochemistry2013
A comparison of DNA compaction by arginine and lysine peptides: a physical basis for arginine rich protamines.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 117 citations in OpenAlex.
- Review
- Nanomechanical response of peptide-bound DNA as a model molecular bio-nanocomposite: a steered molecular dynamics study.Journal of molecular modeling · 2026Article
- Nanostructure and Collagen-Stimulating Activity of Cationic Pentapeptide Lipopeptides.Journal of peptide science : an official publication of the European Peptide Society · 2026Article
- Protein arginine methyltransferases as regulators of phase separation: implications in cancer and neurodegenerative diseases.European biophysics journal : EBJ · 2026Review
- Article
- Histone H3 tail charge patterns govern nucleosome condensate formation and dynamics.Nucleic acids research · 2026Article
- Regulation of STING activation by phosphoinositide and cholesterol.bioRxiv : the preprint server for biology · 2025Article
- Multiple human enhancer RNAs contain long translated open reading frames.Genes & development · 2025Article
- Smart coacervate microdroplets: biomimetic design, material innovations, and emerging applications in biomacromolecule delivery.Bioactive materials · 2025Review
- Protamine Drives Liquid and Solid Condensation of DNA and Glycosaminoglycans.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- The Role of Counterions in the Assembly of Charged Virus-Like Shells.The journal of physical chemistry. B · 2025Article
- Molecular and Computational Studies Reveal That Per- and Polyfluoroalkyl Substances Can Impair Protamine-DNA Interaction, Potentially Inducing DNA Damage.Biomolecules · 2025Article
- Unlocking a Biological Interface of Chiral Supramolecular Helical Polymers.Journal of the American Chemical Society · 2025Article
- Thermodynamics of arginine interactions with organic phosphates.Biophysical journal · 2025Article
- Histone H3 tail charge patterns govern nucleosome condensate formation and dynamics.bioRxiv : the preprint server for biology · 2025Article
- Polymers for Disrupting Protein-Protein Interactions: Where Are We and Where Should We Be?Biomacromolecules · 2024Review
- A DNA condensation code for linker histones.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Dimeric Metal-Salphen Complexes Which Target Multimeric G-Quadruplex DNA.Bioconjugate chemistry · 2023Article
- New Insights into the Role of Ligand-Binding Modes in GC-DNA Condensation through Thermodynamic and Spectroscopic Studies.ACS omega · 2023Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Protamines are small, highly positively charged peptides used to package DNA at very high densities in sperm nuclei. Tight DNA packing is considered essential for the minimization of DNA damage by mutagens and reactive oxidizing species. A striking and general feature of protamines is the almost exclusive use of arginine over lysine for the positive charge to neutralize DNA. We have investigated whether this preference for arginine might arise from a difference in DNA condensation by arginine and lysine peptides. The forces underlying DNA compaction by arginine, lysine, and ornithine peptides are measured using the osmotic stress technique coupled with X-ray scattering. The equilibrium spacings between DNA helices condensed by lysine and ornithine peptides are significantly larger than the interhelical distances with comparable arginine peptides. The DNA surface-to-surface separation, for example, is some 50% larger with polylysine than with polyarginine. DNA packing by lysine rich peptides in sperm nuclei would allow much greater accessibility to small molecules that could damage DNA. The larger spacing with lysine peptides is caused by both a weaker attraction and a stronger short-range repulsion relative to that of the arginine peptides. A previously proposed model for binding of polyarginine and protamine to DNA provides a convenient framework for understanding the differences between the ability of lysine and arginine peptides to assemble DNA.
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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.