journal article·2004-01-01Open access

Effects of polyrotaxane structure on polyion complexation with DNA

Tooru Ooya, Atsushi Yamashita, Motoichi Kurisawa, Yuko Sugaya, Atsushi Maruyama, Nobuhiko Yui

Abstract

Aminoethylcarbamoyl-polyrotaxanes (AEC-α/E35-TYR-Zs) were synthesized as a novel cationic polymer for DNA complexation and characterized in terms of physicochemical properties of polyion complex. Here, AEC groups were introduced to hydroxyl groups of α-cyclodextrins (α-CDs) that are threaded onto a poly(ethylene glycol) (PEG) chain capped with bulky end-groups (polyrotaxane). We examined the ability of DNA complexation of the AEC-α/E35-TYR-Zs compared with polyethylenimine (PEI). Agarose gel shift assay and ethydium bromide (EB) displacement analysis showed that the number of threading α-CDs was one of the dominant factors to enhance the ability of DNA complexation. In addition, increasing the number of AEC groups in the AEC-α/E35-TYR-Zs led to tighter complexation.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: RNA Interference and Gene Delivery · DNA and Nucleic Acid Chemistry · Biopolymer Synthesis and Applications

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan

Institute of Bioengineering and Nanotechnology, 51 Science Park Road #01-01/10, The Aries, Singapore Science Park II, Singapore 117586, Singapore

Department of Biomolecular Engineering, Faculty of Bioscience and Biotechnology Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, Kanagawa 226-8501, Japan

PRESTO, Japan Science and Technology Agency, 4259 Nagatsuta, Midori, Yokohama, Ishikawa 226-8501, Japan

References (32)

Show source-provided references
1. R.G. Crystal, Science 270 (1995) 404–410.10.1126/science.270.5235.404 ↗
2. J. Zabner, A.J. Fasbender, T. Moninger, K.A. Pollinger, M.J. Welsh, J. Biol. Chem. 270 (1995) 18997–19007.10.1074/jbc.270.32.18997 ↗
3. H. Pollard, J.S. Remy, G. Loussouarn, S. Domeolombe, D. Behr, J. Biol. Chem. 273 (1998) 7507–7511.10.1074/jbc.273.13.7507 ↗
4. J. Smisterova, A. Wagenaar, M.C.A. Stuart, E. Polushkin, G.T. Brinke, R. Hulst, J.B.F.N. Engberts, D. Houekstra, J. Biol. Chem. 276 (2001) 47615–47622.10.1074/jbc.M106199200 ↗
5. A. Akinc, R. Langer, Biotech. Bioengng 78 (2002) 503–508.10.1002/bit.20215 ↗
6. C. Pichon, E.L. Cam, B. Guerin, D. Coulaud, E. Delain, P. Midoux, Bioconjug. Chem. 13 (2002) 76–82.10.1021/bc015503o ↗
7. D. Putnam, C.A. Gentry, D.W. Pack, R. Langer, Proc. Natl Acad. Sci. USA 98 (2002) 1200–1205.10.1073/pnas.98.3.1200 ↗
8. M.A. Wolfert, P.R. Dash, O. Nazarova, D. Oupicky, L.W. Seymour, S. Smart, J. Strohalm, K. Ulbrich, Bioconjug. Chem. 10 (1999) 993–1004.10.1021/bc990025r ↗
9. C. Plank, M.X. Tang, A.R. Wolfe, F.C. Szoka, Human Gene Ther. 10 (1999) 319–332.10.1089/10430349950019101 ↗
10. S. Ohashi, T. Kubo, T. Ikeda, Y. Arai, K. Takahashi, Y. Hirasawa, M. Takigawa, E. Satoh, J. Imanishi, O. Mazda, J. Orthop. Sci. 6 (2001) 75–81.10.1007/s007760170028 ↗
11. M.X. Tang, F.C. Szoka, Gene Ther. 4 (1997) 823–932.10.1038/sj.gt.3300454 ↗
12. A. Maruyama, H. Watanabe, A. Ferdous, M. Katoh, T. Ishihara, T. Akaike, Bioconjug. Chem. 9 (1998) 292–299.10.1021/bc9701510 ↗
13. T. Yamaoka, T. Kimura, R. Iwase, A. Murakami, Chem. Lett. (2000) 118–119.10.1246/cl.2000.118 ↗
14. R. Kirvheis, L. Wightman, E. Wanger, Adv. Drug Deliv. Rev. 53 (2001) 341–358.10.1016/S0169-409X(01)00202-2 ↗
15. W.T. Godbey, K.K. Wu, A.G. Mikos, Proc. Natl Acad. Sci. USA 96 (1999) 5177–5181.10.1073/pnas.96.9.5177 ↗
16. M.X. Tang, C.T. Redemann, F.C. Szoka, In vitro gene delivery by degraded polyamidoamine dendrimers, Bioconjug. Chem. 7 (1996) 703–714.10.1021/bc9600630 ↗
17. J. Haensler, F.C. Szoka, Polyamidoamine dendrimers mediate efficient transfection of cells in culture, Bioconjug. Chem. 4 (1993) 372–379.10.1021/bc00023a012 ↗
18. W.T. Godbey, K.K. Wu, A.G. Mikos, Proc. Natl Acad. Sci. USA 96 (1999) 5177–5181.10.1073/pnas.96.9.5177 ↗
19. F. Kihara, H. Arima, T. Tsutsumi, F. Hirayama, K. Uekama, Bioconjug. Chem. 13 (2002) 1211–1219.10.1021/bc025557d ↗
20. T. Ooya, N. Yui, Crit. Rev. Ther. Drug Carrier Syst. 16 (1999) 289–330.10.1615/CritRevTherDrugCarrierSyst.v16.i3.20 ↗
21. T. Ooya, H. Mori, M. Terano, N. Yui, Macromol. Rapid Commun. 16 (1995) 259–263.10.1002/marc.1995.030160405 ↗
22. J. Watanabe, T. Ooya, N. Yui, Chem. Lett. (1998) 1031–1032.10.1246/cl.1998.1031 ↗
23. T. Ooya, N. Yui, J. Biomater. Sci. Polym. Ed. 8 (1997) 437–455.10.1163/156856297X00371 ↗
24. T. Ooya, N. Eguchi, Biomacromolecules 2 (2001) 200–203.10.1021/bm005618f ↗
25. T. Ooya, M. Eguchi, A. Ozaki, N. Yui, Int. J. Pharm. 242 (2002) 47–54.10.1016/S0378-5173(02)00139-4 ↗
26. Y. Ohtani, T. Irie, K. Uekama, K. Fukunaga, J. Pitha. Eur. J. Biochem. 186 (1989) 17–22.10.1111/j.1432-1033.1989.tb15171.x ↗
27. T. Ooya, N. Yui, J. Control. Release 80 (2002) 219–228.10.1016/S0168-3659(02)00030-5 ↗
28. T. Ooya, M. Eguchi, N. Yui, J. Am. Chem. Soc. 125 (2003) 13016–13017.10.1021/ja034583z ↗
29. A. Harada, J. Li, M. Kamachi, J. Am. Chem. Soc. 116 (1994) 3192–3196.10.1021/ja00087a004 ↗
30. M. Chalfie, Y. Tu, G. Euskirchen, W.W. Ward, D.C. Prasher, Science 263 (1994) 802–805.10.1126/science.8303295 ↗
31. A.L. Parker, D. Oupicky, P.R. Dash, L.W. Seymor, Anal. Biochem. 302 (2002) 75–80.10.1006/abio.2001.5507 ↗
32. T. Ooya, N. Yui, Macromol. Chem. Phys. 199 (1998) 2311–2320.10.1002/(SICI)1521-3935(19981001)199:10<2311::AID-MACP2311>3.0.CO;2-T ↗