2004Journal of the American Chemical SocietyRequires access

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

Open publisher page 9 citations

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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What this paper is about

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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OpenAlex reports 9 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available 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.

Key concepts: Internalization, Chemistry, Peptide, Cell-penetrating peptide, Biophysics, Dimer, Mechanism of action, Mechanism (biology)

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