ArticleBiophysical journal2022
Effect of phosphorylation of protamine-like cationic peptide on the binding affinity to DNA.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- From chromosomal protein disorder to chromatin phase separation.Epigenetics & chromatin · 2026Review
- In silico evaluation of FDA-approved antivirals and corticosteroids against SARS-CoV-2.Scientific reports · 2026Article
- Structural Dynamics of Peptiplexes Formed between Cationic Cell-Penetrating Peptides and DNA: A Comparative Study on TAT-HIV and NLS-SV40T.ACS applied bio materials · 2026Article
- In silico identification of potential inhibitors from fenugreek against the pro-inflammatory cytokine IL-17 and its receptor.Odontology · 2026Article
- Cell penetrating peptide-functionalized small interfering RNA nanoparticles knock down HER expression in breast cancer cells.The Journal of pharmacology and experimental therapeutics · 2025Article
- Multiphasic Organization and Differential Dynamics of Proteins within Protein-DNA Biomolecular Condensates.The journal of physical chemistry. B · 2025Article
- Phosphorylation of the protamine-like protein from baculovirus affects its DNA binding and virus propagation.Nucleic acids research · 2025Article
- Insights on the binding mechanisms and structural dynamics of protamine-DNA interaction.Biophysical reviews · 2025Review
- Single-molecule measurements of double-stranded DNA condensation.Biophysical journal · 2025Review
- DNA-protamine condensates under low salt conditions: molecular dynamics simulation with a simple coarse-grained model focusing on electrostatic interactions.Nanoscale advances · 2023Article
- Innovations in biophysics: A sampling of ideas celebrating Ned Seeman's legacy.Biophysical journal · 2022Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protamines are more arginine-rich and more basic than histones and are responsible for providing a highly compacted shape to the sperm heads in the testis. Phosphorylation and dephosphorylation are two events that occur in the late phase of spermatogenesis before the maturation of sperms. In this work, we have studied the effect of phosphorylation of protamine-like cationic peptides using all-atom molecular dynamics simulations. Through thermodynamic analyses, we found that phosphorylation reduces the binding efficiency of such cationic peptides on DNA duplexes. Peptide phosphorylation leads to a less efficient DNA condensation, due to a competition between DNA-peptide and peptide-peptide interactions. We hypothesize that the decrease of peptide bonds between DNA together with peptide self-assembly might allow an optimal re-organization of chromatin and an efficient condensation through subsequent peptide dephosphorylation. Based on the globular and compact conformations of phosphorylated peptides mediated by arginine-phosphoserine H-bonding, we furthermore postulate that phosphorylated protamines could more easily intrude into chromatin and participate to histone release through disruption of histone-histone and histone-DNA binding during spermatogenesis.
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