A Dimerization “Switch” in the Internalization Mechanism of a Cell-Penetrating Peptide
Jason A. Moss, Antonietta M. Lillo, Young Soo Kim, Changshou Gao, Henrik J. Ditzel, Kim D. Janda
Abstract
Jason A. Moss, Antonietta M. Lillo, Young Soo Kim, Changshou Gao, Henrik J. Ditzel, Kim D. Janda
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.
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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.
Key concepts: Internalization, Chemistry, Peptide, Cell-penetrating peptide, Biophysics, Dimer, Mechanism of action, Mechanism (biology)