Nona-Arginine Facilitates Delivery of Quantum Dots into Cells via Multiple PathwaysReport as inadecuate




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Journal of Biomedicine and BiotechnologyVolume 2010 2010, Article ID 948543, 11 pages

Research Article

Department of Biological Sciences, Missouri University of Science and Technology, 105 Schrenk Hall, 400 W. 11th Street, Rolla, MO 65409, USA

Department of Natural Resources and Environmental Studies and Institute of Biotechnology, National Dong Hwa University, Hualien 97401, Taiwan

Department of Chemistry, Missouri University of Science and Technology, 142 Schrenk Hall, 400 W. 11th Street, Rolla, MO 65409, USA

Department of Life Science, National Taiwan Normal University, 88 Ting-Chow Road, Section 4, Taipei 116, Taiwan

Institute of Biotechnology, National Dong Hwa University, Hualien 97401, Taiwan

Received 26 April 2010; Revised 3 August 2010; Accepted 26 September 2010

Academic Editor: Lokesh Joshi

Copyright © 2010 Yi Xu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.





Author: Yi Xu, Betty Revon Liu, Han-Jung Lee, Katie B. Shannon, Jeffrey G. Winiarz, Tien-Chun Wang, Huey-Jenn Chiang, and Yue-wern

Source: https://www.hindawi.com/



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