A Dimerization “Switch” in the Internalization Mechanism of a Cell-Penetrating Peptide
Journal of the American Chemical Society2004Vol. 127(2), pp. 538–539
Citations Over Time
Abstract
The internalization mechanism of a cell-penetrating peptide has been explored through combinatorial selection of a phage-displayed peptide dimer library, chemical synthesis, and biophysical characterization. Both energy-dependent and energy-independent modes for peptide uptake by the target mammalian cells were observed, suggesting a role for higher-order structure in modulating the action of this novel cell-penetrating peptide.
Related Papers
- → Phage display: Concept, innovations, applications and future(2010)480 cited
- → Novel peptides binding to the Fc-portion of immunoglobulins obtained from a combinatorial phage display peptide library(1998)20 cited
- → A Contiguous Stretch of Methionine Residues Mediates the Energy-Dependent Internalization Mechanism of a Cell-Penetrating Peptide(2005)4 cited
- Potential GM-CSF Antagonists Selected from a Peptide Phage Display Library.(1999)
- → Identification of an Indiscriminate Peptide by Phage Display Technology(2020)