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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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B-Lymphocytes / metabolism
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Bacteriophages / metabolism
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Cell Membrane / chemistry
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Cell Membrane / metabolism
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Cell Membrane Permeability
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Dimerization
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Enzyme-Linked Immunosorbent Assay
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Microscopy, Fluorescence
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Molecular Sequence Data
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Oligopeptides / pharmacokinetics
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Peptide Library*
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Protein Conformation
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Proto-Oncogene Proteins c-jun / chemistry
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Proto-Oncogene Proteins c-jun / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Structure-Activity Relationship
Substances
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Oligopeptides
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Peptide Library
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Proto-Oncogene Proteins c-jun
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Recombinant Fusion Proteins