Cell-Penetrating Peptides as Delivery Vehicles for a Protein-Targeted Terbium Complex

Release after transmission: Arginine‐rich, cell‐penetrating peptides (CPPs) mediate cytoplasmic delivery of trimethoprim (TMP)–terbium complex conjugates and selective, intracellular labeling of E. coli dihydrofolate reductase (eDHFR) fusion proteins. A disulfide bond linking CPP and cargo is reduce...

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Bibliographic Details
Published in:Chemistry : a European journal 2012-08, Vol.18 (35), p.10825-10829
Main Authors: Mohandessi, Shabnam, Rajendran, Megha, Magda, Darren, Miller, Lawrence W.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Arginine - chemistry
Arginine - metabolism
Cell Line
Cell Membrane Permeability
Cell-Penetrating Peptides - chemistry
Cell-Penetrating Peptides - metabolism
Chemistry
Dogs
Drug Carriers - chemistry
Drug Carriers - metabolism
Endocytosis
Escherichia coli
Fluorescent Dyes
fluorescent probes
lanthanides
Luminescent Proteins - chemistry
Luminescent Proteins - metabolism
microscopy
Molecular Imaging
Molecular Sequence Data
peptides
protein labeling
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Staining and Labeling
Terbium - chemistry
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Summary:Release after transmission: Arginine‐rich, cell‐penetrating peptides (CPPs) mediate cytoplasmic delivery of trimethoprim (TMP)–terbium complex conjugates and selective, intracellular labeling of E. coli dihydrofolate reductase (eDHFR) fusion proteins. A disulfide bond linking CPP and cargo is reduced following uptake (see picture). CPP conjugation can be used to deliver otherwise cell‐impermeable, ligand–fluorophore conjugates.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.201201805