A Contiguous Stretch of Methionine Residues Mediates the Energy-Dependent Internalization Mechanism of a Cell-Penetrating Peptide
Molecular Pharmaceutics2005Vol. 2(6), pp. 528–535
Citations Over Time
Abstract
Recently we characterized an unusual switch in the internalization mechanism of the monomeric and dimeric forms of the cell-penetrating peptide RDLWEMMMVSLACQY. Here, we observed both energy-dependent and energy-independent modes of peptide uptake by the target B-lymphocytes WI-L2-729HF2, suggesting that higher-order structure might modulate the action of this novel cell-penetrating peptide. In the present work, we propose a possible internalization mechanism for the dimeric peptide which involves an initial interaction with the cell membrane, followed by an energy-dependent internalization process which requires the contiguous Met(6-8) sequence.
Related Papers
- → Distinct Uptake Routes of Cell-Penetrating Peptide Conjugates(2008)180 cited
- → Oligonucleotide Delivery with Cell Surface Binding and Cell Penetrating Peptide Amphiphile Nanospheres(2015)34 cited
- → Enhanced intracellular peptide delivery by multivalent cell-penetrating peptide with bioreducible linkage(2017)23 cited
- → A Contiguous Stretch of Methionine Residues Mediates the Energy-Dependent Internalization Mechanism of a Cell-Penetrating Peptide(2005)4 cited
- Investigation of amino acid sequence of specific ouabain conjugated peptides(2004)