A dimerization "switch" in the internalization mechanism of a cell-penetrating peptide.
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.
Moss
Jason A
JA
Departments of Chemistry and Immunology, The Scripps Research Institute and The Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Lillo
Antonietta
A
Kim
Young Soo
YS
Gao
Changshou
C
Ditzel
Henrik
H
Janda
Kim D
KD
D000595:Amino Acid Sequence; D001402:B-Lymphocytes / Q000378:metabolism; D001435:Bacteriophages / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002463:Cell Membrane Permeability; D019281:Dimerization; D004797:Enzyme-Linked Immunosorbent Assay; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism* / Q000493:pharmacokinetics; D019151:Peptide Library; D011487:Protein Conformation; D016755:Proto-Oncogene Proteins c-jun / Q000737:chemistry / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D019151:Peptide Library; D016755:Proto-Oncogene Proteins c-jun; D011993:Recombinant Fusion Proteins