ArticleBiophysical journal2010
Influence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 87 citations in OpenAlex.
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- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
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- Coarse-Grained Molecular Dynamics of pH-Sensitive Lipids.International journal of molecular sciences · 2023Article
- Membrane-mediated protein interactions drive membrane protein organization.Nature communications · 2022Article
- A Core-Shell Approach for Systematically Coarsening Nanoparticle-Membrane Interactions: Application to Silver Nanoparticles.Nanomaterials (Basel, Switzerland) · 2022Article
- Modeling Receptor Motility along Advecting Lipid Membranes.Membranes · 2022Review
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- Unraveling the complex enzymatic machinery making a key galactolipid in chloroplast membrane: a multiscale computer simulation.Scientific reports · 2020Article
- A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes.Chembiochem : a European journal of chemical biology · 2020Article
- Understanding biochemical processes in the presence of sub-diffusive behavior of biomolecules in solution and living cells.Biophysical reviews · 2019Review
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- Emerging roles for sphingolipids in cellular aging.Current genetics · 2018Review
- Sphingolipids facilitate age asymmetry of membrane proteins in dividing yeast cells.Molecular biology of the cell · 2017Article
- Effects of Coarse Graining and Saturation of Hydrocarbon Chains on Structure and Dynamics of Simulated Lipid Molecules.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the effect of amino acid composition and hydrophobic length of alpha-helical transmembrane peptides and the role of electrostatic interactions on the lateral diffusion of the peptides in lipid membranes. Model peptides of varying length and composition, and either tryptophans or lysines as flanking residues, were synthesized. The peptides were labeled with the fluorescent label Alexa Fluor 488 and incorporated into phospholipid bilayers of different hydrophobic thickness and composition. Giant unilamellar vesicles were formed by electroformation, and the lateral diffusion of the transmembrane peptides (and lipids) was determined by fluorescence correlation spectroscopy. In addition, we performed coarse-grained molecular-dynamics simulations of single peptides of different hydrophobic lengths embedded in planar membranes of different thicknesses. Both the experimental and simulation results indicate that lateral diffusion is sensitive to membrane thickness between the peptides and surrounding lipids. We did not observe a difference in the lateral diffusion of the peptides with respect to the presence of tryptophans or lysines as flanking residues. The specific lipid headgroup composition of the membrane has a much less pronounced impact on the diffusion of the peptides than does the hydrophobic thickness.
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