ArticleBiochemistry2010
Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 104 citations in OpenAlex.
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- Recent Advances of Studies on Cell-Penetrating Peptides Based on Molecular Dynamics Simulations.Cells · 2022Review
- Arginine Homopeptide of 11 Residues as a Model of Cell-Penetrating Peptides in the Interaction with Bacterial Membranes.Membranes · 2022Article
- Membrane Internalization Mechanisms and Design Strategies of Arginine-Rich Cell-Penetrating Peptides.International journal of molecular sciences · 2022Review
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- Predicting cell-penetrating peptides using machine learning algorithms and navigating in their chemical space.Scientific reports · 2021Article
- The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020Article
- Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage.Nature communications · 2020Article
- Exploiting heterogeneous time scale of dynamics to enhance 2D HETCOR solid-state NMR sensitivity.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Improving cellular uptake of therapeutic entities through interaction with components of cell membrane.Drug delivery · 2019Review
- Antimicrobial peptide ROAD-1 triggers phase change in local membrane environment to execute its activity.Journal of molecular modeling · 2019Article
- Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog.Communications biology · 2019Article
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
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- Glycosaminoglycan Binding and Non-Endocytic Membrane Translocation of Cell-Permeable Octaarginine Monitored by Real-Time In-Cell NMR Spectroscopy.Pharmaceuticals (Basel, Switzerland) · 2017Article
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- Mechanism Matters: A Taxonomy of Cell Penetrating Peptides.Trends in biochemical sciences · 2015Review
- Structural Changes and Proapoptotic Peroxidase Activity of Cardiolipin-Bound Mitochondrial Cytochrome c.Biophysical journal · 2015Article
- Frequency-selective REDOR and spin-diffusion relays in uniformly labeled whole cells.Solid state nuclear magnetic resonance · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The protein transduction domain of HIV-1 TAT, TAT(48-60), is an efficient cell-penetrating peptide (CPP) that diffuses across the lipid membranes of cells despite eight cationic Arg and Lys residues. To understand its mechanism of membrane translocation against the free energy barrier, we have conducted solid-state NMR experiments to determine the site-specific conformation, dynamics, and lipid interaction of the TAT peptide in anionic lipid bilayers. We found that TAT(48-60) is a highly dynamic and nearly random coil peptide in the lipid bilayer and inserts into the membrane-water interface near the glycerol backbone region. Arg-phosphate salt bridge interaction was revealed by short guanidinium-phosphate distances and restricted dynamics of the guanidinium. Together with the observation of strong peptide-water cross-peaks in (1)H spin diffusion spectra, these results indicate that TAT binding to the membrane-water interface is stabilized not only by electrostatic attraction to the anionic lipids but also by intermolecular hydrogen bonding with the lipid phosphates and water, which may take the role of intramolecular hydrogen bonds in canonical secondary structures. The random coil structure of TAT and another CPP, penetratin, suggests that the lack of amphipathic structure is essential for rapid translocation of these Arg-rich CPPs across the lipid membrane without causing permanent damages to the membrane integrity.
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