ArticleBiochemistry2008
Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Leaflet-Dependent Effect of Anionic Lipids on Membrane Insertion by Cationic Cell-Penetrating Peptides.The journal of physical chemistry letters · 2023Article
- Cell-Penetrating Peptides and Transportan.Pharmaceutics · 2021Review
- The role of membrane tension in the action of antimicrobial peptides and cell-penetrating peptides in biomembranes.Biophysical reviews · 2019Review
- Membrane Active Peptides and Their Biophysical Characterization.Biomolecules · 2018Review
- Daptomycin-Phosphatidylglycerol Domains in Lipid Membranes.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Charge Distribution Fine-Tunes the Translocation of α-Helical Amphipathic Peptides across Membranes.Biophysical journal · 2016Article
- Mechanism Matters: A Taxonomy of Cell Penetrating Peptides.Trends in biochemical sciences · 2015Review
- 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
- Translocation of cationic amphipathic peptides across the membranes of pure phospholipid giant vesicles.Journal of the American Chemical Society · 2013Article
- What determines the activity of antimicrobial and cytolytic peptides in model membranes.Biochemistry · 2011Article
- Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer.The journal of physical chemistry. B · 2011Article
- A thermodynamic approach to the mechanism of cell-penetrating peptides in model membranes.Biochemistry · 2011Article
- Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics.Biochemistry · 2009Article
- Wasp mastoparans follow the same mechanism as the cell-penetrating peptide transportan 10.Biochemistry · 2009Article
- The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The kinetics and thermodynamics of binding of transportan 10 (tp10) and four of its variants to phospholipid vesicles, and the kinetics of peptide-induced dye efflux, were compared. Tp10 is a 21-residue, amphipathic, cationic, cell-penetrating peptide similar to helical antimicrobial peptides. The tp10 variants examined include amidated and free peptides, and replacements of tyrosine by tryptophan. Carboxy-terminal amidation or substitution of tryptophan for tyrosine enhance binding and activity. The Gibbs energies of peptide binding to membranes determined experimentally and calculated from the interfacial hydrophobicity scale are in good agreement. The Gibbs energy for insertion into the bilayer core was calculated using hydrophobicity scales of residue transfer from water to octanol and to the membrane/water interface. Peptide-induced efflux becomes faster as the Gibbs energies for binding and insertion of the tp10 variants decrease. If anionic lipids are included, binding and efflux rate increase, as expected because all tp10 variants are cationic and an electrostatic component is added. Whether the most important effect of peptide amidation is the change in charge or an enhancement of helical structure, however, still needs to be established. Nevertheless, it is clear that the changes in efflux rate reflect the differences in the thermodynamics of binding and insertion of the free and amidated peptide groups.
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