ArticleThe journal of physical chemistry. B2011
Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
- A molecular dynamics study of cell-penetrating peptide transportan-10 (TP10): Binding, folding and insertion to transmembrane state in zwitterionic membrane.Biochimica et biophysica acta. Biomembranes · 2024Article
- Recent Advances of Studies on Cell-Penetrating Peptides Based on Molecular Dynamics Simulations.Cells · 2022Review
- Biological Membrane-Penetrating Peptides: Computational Prediction and Applications.Frontiers in cellular and infection microbiology · 2022Review
- Cell-Penetrating Peptides and Transportan.Pharmaceutics · 2021Review
- Transportan 10 improves the pharmacokinetics and pharmacodynamics of vancomycin.Scientific reports · 2019Article
- Targeted Theranostic Nanoparticles for Brain Tumor Treatment.Pharmaceutics · 2018Review
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Coarse-grained simulations of hemolytic peptide δ-lysin interacting with a POPC bilayer.Biochimica et biophysica acta · 2016Article
- Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.Biophysical journal · 2016Article
- A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa.World journal of microbiology & biotechnology · 2016Article
- Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surface.Chemistry and physics of lipids · 2016Article
- Mechanism Matters: A Taxonomy of Cell Penetrating Peptides.Trends in biochemical sciences · 2015Review
- Analysis of the flexibility and stability of the structure of magainin in a bilayer, and in aqueous and nonaqueous solutions using molecular dynamics simulations.Journal of molecular modeling · 2015Article
- Peptides with the same composition, hydrophobicity, and hydrophobic moment bind to phospholipid bilayers with different affinities.The journal of physical chemistry. B · 2014Article
- Membrane-active peptides: binding, translocation, and flux in lipid vesicles.Biochimica et biophysica acta · 2014Review
- Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state.PloS one · 2014Article
- Cell-penetrating peptide secures an efficient endosomal escape of an intact cargo upon a brief photo-induction.Cellular and molecular life sciences : CMLS · 2013Article
- Identification of cell-penetrating peptides that are bactericidal to Neisseria meningitidis and prevent inflammatory responses upon infection.Antimicrobial agents and chemotherapy · 2013Article
- Membrane binding and insertion of a pHLIP peptide studied by all-atom molecular dynamics simulations.International journal of molecular sciences · 2013Article
- Comparative molecular dynamics simulations of the antimicrobial peptide CM15 in model lipid bilayers.Biochimica et biophysica acta · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We performed a series of molecular dynamics simu lations to study the nature of interactions between transportan 10 (tp10) and a zwitterionic POPC bilayer. Tp10 is an amphipathic cell-penetrating peptide with a net positive charge of +5 and is known to adopt an α-helical secondary structure on the surface of POPC membranes. The study showed that tp10 preferentially binds to the membrane surface with its hydrophobic side facing the hydrophobic lipid core. Such orientation allows Lys residues, with positively charged long side chains, to stay in the polar environment during the insertion process. The simulations revealed that the Lys-phosphate salt bridge is a key factor in determining the orientation of the peptide in the interfacial region as well as in stabilizing the peptide-membrane interaction. The electrostatic attraction between Lys and phosphate groups is also believed to be the main bottleneck for the translocation of tp10 across the membrane.
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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.