ArticleBiochemistry2007
Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 65 citations in OpenAlex.
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Structure of the transmembrane domain of human nicastrin-a component of γ-secretase.Scientific reports · 2016Article
- Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells.Scientific reports · 2015Article
- Effects of truncating van der Waals interactions in lipid bilayer simulations.The Journal of chemical physics · 2014Article
- Partial somatic to stem cell transformations induced by cell-permeable reprogramming factors.Scientific reports · 2014Article
- Cell-permeable parkin proteins suppress Parkinson disease-associated phenotypes in cultured cells and animals.PloS one · 2014Article
- NMR-based simulation studies of Pf1 coat protein in explicit membranes.Biophysical journal · 2013Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- Antitumor activity of cell-permeable RUNX3 protein in gastric cancer cells.Clinical cancer research : an official journal of the American Association for Cancer Research · 2013Article
- Antitumor activity of cell-permeable p18(INK4c) with enhanced membrane and tissue penetration.Molecular therapy : the journal of the American Society of Gene Therapy · 2012Article
- Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.Biophysical journal · 2012Article
- Influence of the membrane dipole potential on peptide binding to lipid bilayers.Biophysical chemistry · 2012Article
- ORF8a of SARS-CoV forms an ion channel: experiments and molecular dynamics simulations.Biochimica et biophysica acta · 2011Article
- Probing the spontaneous membrane insertion of a tail-anchored membrane protein by sum frequency generation spectroscopy.Journal of the American Chemical Society · 2010Article
- In vivo islet protection by a nuclear import inhibitor in a mouse model of type 1 diabetes.PloS one · 2010Article
- Coarse grained molecular dynamics simulations of transmembrane protein-lipid systems.International journal of molecular sciences · 2010Review
- Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.Journal of the American Chemical Society · 2010Article
- Retinal dynamics during light activation of rhodopsin revealed by solid-state NMR spectroscopy.Biochimica et biophysica acta · 2010Review
- Tilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy.Biophysical journal · 2009Article
- Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cell-signaling peptides have been extensively used to transport functional molecules across the plasma membrane into living cells. These peptides consist of a hydrophobic sequence and a cationic nuclear localization sequence (NLS). It has been assumed that the hydrophobic region penetrates the hydrophobic lipid bilayer and delivers the NLS inside the cell. To better understand the transport mechanism of these peptides, in this study, we investigated the structure, orientation, tilt of the peptide relative to the bilayer normal, and the membrane interaction of two cell-signaling peptides, SA and SKP. Results from CD and solid-state NMR experiments combined with molecular dynamics simulations suggest that the hydrophobic region is helical and has a transmembrane orientation with the helical axis tilted away from the bilayer normal. The influence of the hydrophobic mismatch, between the hydrophobic length of the peptide and the hydrophobic thickness of the bilayer, on the tilt angle of the peptides was investigated using thicker POPC and thinner DMPC bilayers. NMR experiments showed that the hydrophobic domain of each peptide has a tilt angle of 15 +/- 3 degrees in POPC, whereas in DMPC, 25 +/- 3 degree and 30 +/- 3 degree tilts were observed for SA and SKP peptides, respectively. These results are in good agreement with molecular dynamics simulations, which predict a tilt angle of 13.3 degrees (SA in POPC), 16.4 degrees (SKP in POPC), 22.3 degrees (SA in DMPC), and 31.7 degrees (SKP in DMPC). These results and simulations on the hydrophobic fragment of SA or SKP suggest that the tilt of helices increases with a decrease in bilayer thickness without changing the phase, order, and structure of the lipid bilayers.
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