Semiconductor quantum dots (QDs) have recently been used to deliver and monitor biomolecules, such as drugs and proteins. However, QDs alone have a low efficiency of transport across the plasma membrane. In order to increase the efficiency, we used synthetic nona-arginine (SR9), a cell-penetrating peptide, to facilitate uptake. We found that SR9 increased the cellular uptake of QDs in a noncovalent binding manner between QDs and SR9. Further, we investigated mechanisms of QD/SR9 cellular internalization. Low temperature and metabolic inhibitors markedly inhibited the uptake of QD/SR9, indicating that internalization is an energy-dependent process. Results from both the pathway inhibitors and the RNA interference (RNAi) technique suggest that cellular uptake of QD/SR9 is predominantly a lipid raft-dependent process mediated by macropinocytosis. However, involvement of clathrin and caveolin-1 proteins in transducing QD/SR9 across the membrane cannot be completely ruled out.
- Arginine Derivative,
- Caveolin 1,
- Cell Penetrating Peptide,
- Clathrin,
- Nona Arginine,
- Quantum Dot,
- Unclassified Drug,
- Cadmium Derivative,
- Cadmium Selenide,
- Nonaarginine,
- Selenium Derivative,
- Small Interfering RNA,
- Sulfide,
- Zinc Derivative,
- Zinc Sulfide,
- Cell Membrane,
- Cell Metabolism,
- Controlled Study,
- Energy,
- Human,
- Human Cell,
- Inhibition Kinetics,
- Internalization,
- Lipid Raft,
- Low Temperature,
- RNA Interference,
- Signal Transduction,
- Drug Antagonism,
- Fluorescence Microscopy,
- Genetics,
- Metabolism,
- Methodology,
- Pinocytosis,
- Transport At the Cellular Level,
- Tumor Cell Line,
- Western Blotting,
- Biological Transport,
- Blotting, Western,
- Cadmium Compounds,
- Caveolins,
- Cell Line, Tumor,
- Clathrin Heavy Chains,
- Drug Delivery Systems,
- Humans,
- Microscopy, Fluorescence,
- Oligopeptides,
- RNA, Small Interfering,
- Selenium Compounds,
- Sulfides,
- Zinc Compounds
Available at: http://works.bepress.com/katie_shannon/26/