Abstract |
The internalization of near-infrared fluorescently labeled cargos into living cells and tissues allows a highly sensitive detection without interference from skin, porphins or other fluorescent cell and tissue compounds. In this study, the uptake of labeled bovine serum albumin and an antibody, into fibrosarcoma (HT-1080) cells was triggered by the formation of non-covalent complexes with different cell-penetrating peptides; uptake efficiency and intracellular localization were determined. To improve selectivity of internalization into tumor cells, a fluorescent activatable cell-penetrating peptide (ACPP) was synthesized and functionally characterized. This 25-mer peptide was designed to be activatable by Matrix-Metallo- Proteases ( MMPs). Its uptake selectivity was estimated using cells with different MMP activities.
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Authors | Felista Tansi, Eric Kallweit, Christoph Kaether, Katarina Kappe, Christina Schumann, Ingrid Hilger, Siegmund Reissmann |
Journal | Journal of cellular biochemistry
(J Cell Biochem)
Vol. 116
Issue 7
Pg. 1222-31
(Jul 2015)
ISSN: 1097-4644 [Electronic] United States |
PMID | 25546737
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | © 2014 Wiley Periodicals, Inc. |
Chemical References |
- Carbocyanines
- Cell-Penetrating Peptides
- DY-676
- Fluorescent Dyes
- Indoles
- Serum Albumin, Bovine
- Matrix Metalloproteinases
- Trastuzumab
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Topics |
- Carbocyanines
(chemistry)
- Cell Line, Tumor
- Cell-Penetrating Peptides
(chemical synthesis, pharmacology)
- Drug Delivery Systems
(methods)
- Fluorescent Dyes
(chemistry)
- Humans
- Indoles
(chemistry)
- Matrix Metalloproteinases
(metabolism)
- Serum Albumin, Bovine
(chemistry)
- Trastuzumab
(chemistry, metabolism)
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