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Cell surface binding and uptake of arginine- and lysine-rich penetratin peptides in absence and presence of proteoglycans.
Membrane binding and translocation of cell-penetrating peptides.
- P. Thoren, D. Persson, E. Esbjörner, M. Goksör, P. Lincoln, B. Nordén
- Biology, ChemistryBiochemistry
- 2 March 2004
Under the conditions used in the present study, peptide-lipid interactions alone cannot explain the different cellular uptake characteristics exhibited by these peptides, and the choice of model system is crucial for the conclusions about the ability of CPPs to translocate across lipid membranes.
Template-directed oligonucleotide strand ligation, covalent intramolecular DNA circularization and catenation using click chemistry.
- Ravindra Kumar, A. El-Sagheer, John Tumpane, P. Lincoln, L. M. Wilhelmsson, T. Brown
- Chemistry, BiologyJournal of the American Chemical Society
- 9 May 2007
A template-free click-ligation reaction has been used for the intramolecular circularization of a single stranded oligonucleotide which was used as a template for the synthesis of a covalently closed DNA catenane.
Application of a novel analysis to measure the binding of the membrane-translocating peptide penetratin to negatively charged liposomes.
- D. Persson, P. Thoren, M. Herner, P. Lincoln, B. Nordén
- Chemistry, BiologyBiochemistry
- 21 January 2003
A model based on the Gouy-Chapman theory in combination with a two-state surface partition equilibrium, separating the electrostatic and the hydrophobic contributions to the binding free energy, was found to be in excellent agreement with the experimental data.
Membrane destabilizing properties of cell-penetrating peptides.
Vesicle size-dependent translocation of penetratin analogs across lipid membranes.
Membrane interactions of cell-penetrating peptides probed by tryptophan fluorescence and dichroism techniques: correlations of structure to cellular uptake.
There is a negative correlation between alpha-helical structure and uptake efficiency for penetratin peptides where the two central arginine residues of penetratein are thought to be important for breaking the secondary structure.
Binding of cell-penetrating penetratin peptides to plasma membrane vesicles correlates directly with cellular uptake.
Thread insertion of a bis(dipyridophenazine) diruthenium complex into the DNA double helix by the extrusion of AT base pairs and cross-linking of DNA duplexes.
The crystal structure of the Δ,Δ enantiomer of the binuclear "light-switch" ruthenium complex bound to the oligonucleotide d(CGTACG) shows that one dppz moiety of the dumbbell-like compound inserts into the DNA stack through the extrusion of an AT base pair.