ArticleBiophysical journal2005
Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 67 citations in OpenAlex.
- Penetratin an Old Player in the Field of Cell-Penetrating Peptides Is in New Custom-Effect of Aromatic Non-Natural Amino Acid Substitutions.Pharmaceutics · 2026Article
- 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
- Molecular Dynamics Simulations of Drug-Conjugated Cell-Penetrating Peptides.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Systemic and brain delivery of antidiabetic peptides through nasal administration using cell-penetrating peptides.Frontiers in pharmacology · 2022Review
- Mechanism of interactions between tripeptide NCW on cellular membrane using molecular dynamic simulation.Frontiers in nutrition · 2022Article
- Effect of monovalent salt concentration and peptide secondary structure in peptide-micelle binding.RSC advances · 2021Article
- Biophysical Insight on the Membrane Insertion of an Arginine-Rich Cell-Penetrating Peptide.International journal of molecular sciences · 2019Article
- Article
- Region-Dependent Role of Cell-Penetrating Peptides in Insulin Absorption Across the Rat Small Intestinal Membrane.The AAPS journal · 2015Article
- Peptide-ligand binding modeling of siRNA with cell-penetrating peptides.BioMed research international · 2014Article
- Investigation of homeodomain membrane translocation properties: insights from the structure determination of engrailed-2 homeodomain in aqueous and membrane-mimetic environments.Biophysical journal · 2013Article
- Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.The journal of physical chemistry. B · 2011Article
- Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR.Biochemistry · 2010Article
- Identification of specific lipid-binding sites in integral membrane proteins.The Journal of biological chemistry · 2010Article
- Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers.Biophysical journal · 2009Article
- Pore formation induced by an antimicrobial peptide: electrostatic effects.Biophysical journal · 2008Article
- Article
- Interaction of protegrin-1 with lipid bilayers: membrane thinning effect.Biophysical journal · 2006Article
- A model structure for the heterodimer apoA-IMilano-apoA-II supports its peculiar susceptibility to proteolysis.Biophysical journal · 2006Article
- Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions.Biochimica et biophysica acta · 2006Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using molecular dynamics simulations, we studied the mode of association of the cell-penetrating peptide penetratin with both a neutral and a charged bilayer. The results show that the initial peptide-lipid association is a fast process driven by electrostatic interactions. The homogeneous distribution of positively charged residues along the axis of the helical peptide, and especially residues K46, R53, and K57, contribute to the association of the peptide with lipids. The bilayer enhances the stability of the penetratin helix. Oriented parallel to the lipid-water interface, the subsequent insertion of the peptide through the bilayer headgroups is significantly slower. The presence of negatively charged lipids considerably enhances peptide binding. Lateral side-chain motion creates an opening for the helix into the hydrophobic core of the membrane. The peptide aromatic residues form a pi-stacking cluster through W48/R52/W56 and F49/R53, protecting the peptide from the water phase. Interaction with the penetratin peptide has only limited effect on the overall membrane structure, as it affects mainly the conformation of the lipids which interact directly with the peptide. Charge matching locally increases the concentration of negatively charged lipids, lateral lipid diffusion locally decreases. Lipid disorder increases, through decreased order parameters of the lipids interacting with the penetratin side chains. Penetratin molecules at the membrane surface do not seem to aggregate.
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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.