Targeting of EGF-displayed protein nanoparticles with anticancer drugs
Rie Matsumoto
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorRieko Hara
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorTakashi Andou
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorMasayasu Mie
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorCorresponding Author
Eiry Kobatake
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Correspondence to: E. Kobatake (e-mail: [email protected])Search for more papers by this authorRie Matsumoto
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorRieko Hara
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorTakashi Andou
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorMasayasu Mie
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Search for more papers by this authorCorresponding Author
Eiry Kobatake
Department of Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8502 Japan
Correspondence to: E. Kobatake (e-mail: [email protected])Search for more papers by this authorThis article was published online on 3 April 2014. An error was subsequently identified. This notice is included in the online and print versions to indicate that both have been corrected on 20 August 2014.
Abstract
The development of protein-based carriers for drug delivery has been well studied. We previously constructed a protein-based nanoparticle consisting of genetically engineered elastin-like polypeptides (ELPs) with a fused poly-aspartic acid tail (ELPD). The size of the self-assembled ELPD nanoparticles was regulated by charged repulsion of the poly-aspartic acid chains. In the present study, epidermal growth factor (EGF) was genetically fused to the C-terminus of ELPD to impart an active targeting ability to the ELPD nanoparticles. We examined the nanoparticle formation with EGF as well as its targeting ability. ELPD with fused EGF was found to form nanoparticles that displayed multivalent EGFs on their surface. EGF-displayed nanoparticles loaded with the anti-cancer drug paclitaxel were internalized into cells overexpressing the EGF receptor, and induced cell death. © 2014 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 102B: 1792–1798, 2014.
Supporting Information
Additional Supporting Information may be found in the online version of this article.
| Filename | Description |
|---|---|
| jbmb33162-sup-0001-suppfig01.tif593.2 KB | Supplementary Information Figure 1. |
| jbmb33162-sup-0002-suppfig02.tif2.1 MB | Supplementary Information Figure 2. |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
REFERENCES
- 1Discher DE, Eisenberg A. Polymer vesicles. Science 2002; 297: 967–973.
- 2Oh JK, Drumright R, Siegwart DJ, Matyjaszewski K. The development of microgels/nanogels for drug delivery applications. Prog Polym Sci 2008; 33: 448–477.
- 3Kost J, Langer R. Responsive polymeric delivery systems. Adv Drug Deliver Rev 2012; 64: 327–341.
- 4Kojima C. Design of stimuli-responsive dendrimers. Expert Opin Drug Deliv 2010; 7: 307–319.
- 5Meyer DE, Chilkoti A. Purification of recombinant proteins by fusion with thermally responsive polypeptides. Nat Biotechnol 1999; 17: 1112–1115.
- 6Meyer DE, Trabbic-Carlson K, Chilkoti A. Protein purification by fusion with an environmentally responsive elastin-like polypeptide: Effect of polypeptide length on the purification of thioredoxin. Biotechnol Prog 2001; 17: 720–728.
- 7Urry DW, Parker TM, Reid MC, Gowda DC. Biocompatibility of the bioelastic materials, poly(gvgvp) and its gamma-irradiation cross-linked matrix—Summary of generic biological test-results. J Bioact Compat Polym 1991; 6: 263–282.
- 8Betre H, Liu W, Zalutsky MR, Chilkoti A, Kraus VB, Setton LA. A thermally responsive biopolymer for intra-articular drug delivery. J Control Release 2006; 115: 175–182.
- 9Herrero-Vanrell R, Rincon AC, Alonso M, Reboto V, Molina-Martinez IT, Rodriguez-Cabello JC. Self-assembled particles of an elastin-like polymer as vehicles for controlled drug release. J Control Release 2005; 102: 113–122.
- 10Ciofani G, Genchi GG, Guardia P, Mazzolai B, Mattoli V, Bandiera A. Recombinant human elastin-like magnetic microparticles for drug delivery and targeting. Macromol Biosci 2013. doi: 10.1002/mabi.201300361. [Epub ahead of print].
- 11Hassouneh W, Nunalee ML, Shelton MC, Chilkoti A. Calcium binding peptide motifs from calmodulin confer divalent ion selectivity to elastin-like polypeptides. Biomacromolecules 2013; 14: 2347–2353.
- 12Bressan GM, Pasqualironchetti I, Fornieri C, Mattioli F, Castellani I, Volpin D. Relevance of aggregation properties of tropoelastin to the assembly and structure of elastic fibers. J Ultrastruct Mol Struct Res 1986; 94: 209–216.
- 13Dreher MR, Simnick AJ, Fischer K, Smith RJ, Patel A, Schmidt M, Chilkoti A. Temperature triggered self-assembly of polypeptides into multivalent spherical micelles. J Am Chem Soc 2008; 130: 687–694.
- 14Fujita Y, Mie M, Kobatake E. Construction of nanoscale protein particle using temperature-sensitive elastin-like peptide and polyaspartic acid chain. Biomaterials 2009; 30: 3450–3457.
- 15Simnick AJ, Valencia CA, Liu RH, Chilkoti A. Morphing low-affinity ligands into high-avidity nanoparticles by thermally triggered self-assembly of a genetically encoded polymer. Acs Nano 2010; 4: 2217–2227.
- 16Simnick AJ, Amiram M, Liu WG, Hanna G, Dewhirst MW, Kontos CD, Chilkoti A. In vivo tumor targeting by a NGR-decorated micelle of a recombinant diblock copolypeptide. J Control Release 2011; 155: 144–151.
- 17Sun GY, Hsueh PY, Janib SM, Hamm-Alvarez S, MacKay JA. Design and cellular internalization of genetically engineered polypeptide nanoparticles displaying adenovirus knob domain. J Control Release 2011; 155: 218–226.
- 18Sarangthem V, Cho EA, Bae SM, Singh TD, Kim SJ, Kim S, Jeon WB, Lee BH, Park RW. Construction and application of elastin like polypeptide containing IL-4 receptor targeting peptide. PLoS One 2013; 8: e81891.
- 19Paez JG, Jänne PA, Lee JC, Tracy S, Greulich H, Gabriel S, Herman P, Kaye FJ, Lindeman N, Boggon TJ, Naoki K, Sasaki H, Fujii Y, Eck MJ, Sellers WR, Johnson BE, Meyerson M. EGFR mutations in lung cancer: Correlation with clinical response to gefitinib therapy. Science 2004; 304: 1497–1500.
- 20Lynch TJ, Bell DW, Sordella R, Gurubhagavatula S, Okimoto RA, Brannigan BW, Harris PL, Haserlat SM, Supko JG, Haluska FG, Louis DN, Christiani DC, Settleman J, Haber DA. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N Engl J Med 2004; 350: 2129–2139.
- 21McPherson DT, Xu J, Urry DW. Product purification by reversible phase transition following Escherichia coli expression of genes encoding up to 251 repeats of the elastomeric pentapeptide GVGVP. Protein Expr Purif 1996; 7: 51–57.
- 22Rincon AC, Molina-Martinez IT, de Las Heras B, Alonso M, Bailez C, Rodriguez-Cabello JC, Herrero-Vanrell R. Biocompatibility of elastin-like polymer poly(VPAVG) microparticles: In vitro and in vivo studies. J Biomed Mater Res A 2006; 78A: 343–351.
- 23Hassouneh W, Fischer K, MacEwan SR, Branscheid R, Fu CL, Liu RH, Schmidt M, Chilkoti A. Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers. Biomacromolecules 2012; 13: 1598–1605.
- 24De Campos Vidal B. The use of the fluorescent probe 8-anilinonaphthalene sulfate (ANS) for collagen and elastin histochemistry. J Histochem Cytochem 1978; 26: 196–201.
- 25Yui H, Guo Y, Koyama K, Sawada T, John G, Yang B, Masuda M, Shimizu T. Local environment and property of water inside the hollow cylinder of a lipid nanotube. Langmuir 2005; 21: 721–727.
- 26Dautryvarsat A. Receptor-mediated endocytosis—The intracellular journey of transferrin and its receptor. Biochimie 1986; 68: 375–381.
