Phase diagrams of DNA-photosensitive surfactant complexes: Effect of ionic strength and surfactant structure

Journal of Chemical Physics

Volumn 141, Issue 16, 2014, Pages

  Zakrevskyy, Yuriy ^a,b   Titov, Evgenii ^a   Lomadze, Nino ^a   Santer, Svetlana ^a  

^a UNIVERSITY OF POTSDAM   (Germany)

^b Gummersbach Campus   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

COMPACTION; DNA; HYDROPHOBICITY; LIGHT SENSITIVE MATERIALS; PHASE DIAGRAMS; PHOTOSENSITIVITY; SHIMS; SODIUM CHLORIDE; SURFACE ACTIVE AGENTS;

COMPACTION MECHANISMS; EFFECT OF IONIC STRENGTH; ENVIRONMENTAL PARAMETER; OPTICALLY CONTROLLED; SUBSTANTIAL REDUCTION; SURFACTANT COMPLEXES; SURFACTANT CONCENTRATIONS; SURFACTANT HYDROPHOBICITY;

IONIC STRENGTH;

AZO COMPOUND; AZOBENZENE; DNA; SURFACTANT;

CHEMICAL PHENOMENA; CHEMISTRY; CONFORMATION; LIGHT; OSMOLARITY;

AZO COMPOUNDS; DNA; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGHT; NUCLEIC ACID CONFORMATION; OSMOLAR CONCENTRATION; SURFACE-ACTIVE AGENTS;

EID: 84908441429     PISSN: 00219606     EISSN: 10897690     Source Type: Journal    
DOI: 10.1063/1.4899281     Document Type: Article

References (45)

1. T. Niidome and L. Huang, Gene Therapy 9, 1647 (2002). 10.1038/sj.gt.3301923
2. M. Thomas and A. Klibanov, Appl. Microbiol. Biotechnol. 62, 27 (2003). 10.1007/s00253-003-1321-8
3. B. Demeneix, Z. Hassani, and J.-P. Behr, Curr. Gene Ther. 4, 445 (2004). 10.2174/1566523043345940
4. S. Hart, Cell Biol. Toxicol. 26, 69 (2010). 10.1007/s10565-009-9141-y
5. DNA Interactions with Polymers and Surfactants, edited by R. Dias and B. Lindman (John Wiley and Sons Ltd., 2008).
6. V. Bloomfield, Biopolymers 31, 1471 (1991). 10.1002/bip.360311305
7. V. Bloomfield, Biopolymers 44, 269 (1997). 10.1002/(SICI)1097-0282(1997)44:3<269::AID-BIP6>3.0.CO;2-T
8. M. Suwalsky, W. Traub, U. Shmueli, and J. Subirana, J. Mol. Biol. 42, 363 (1969). 10.1016/0022-2836(69)90049-7
9. L. Gosule and J. Schellman, Nature (London) 259, 333 (1976). 10.1038/259333a0
10. I. Baeza, P. Gariglio, L. Rangel, P. Chavez, L. Cervantes, C. Arguello, C. Wong, and C. Montanez, Biochemistry 26, 6387 (1987). 10.1021/bi00394a012
11. M. Takahashi, K. Yoshikawa, V. Vasilevskaya, and A. Khokhlov, J. Phys. Chem. B 101, 9396 (1997). 10.1021/jp9716391
12. M. Hsiang and R. Cole, Proc. Natl. Acad. Sci. U.S.A. 74, 4852 (1977). 10.1073/pnas.74.11.4852
13. M. Garcia-Ramirez and J. Subirana, Biopolymers 34, 285 (1994). 10.1002/bip.360340214
14. W. Chen, N. Turro, and D. Tomalia, Langmuir 16, 15 (2000). 10.1021/la981429v
15. M. Ainalem and T. Nylander, Soft Matter 7, 4577 (2011). 10.1039/c0sm01171a
16. A. Zinchenko, K. Yoshikawa, and D. Baigl, Phys. Rev. Lett. 95, 228101 (2005). 10.1103/PhysRevLett.95.228101
17. T. Zhou, A. Llizo, C. Wang, G. Xu, and Y. Yang, Nanoscale 5, 8288 (2013). 10.1039/c3nr01630g
18. U. Laemmli, J. Paulson, and V. Hitchins, J. Supramol. Struct. 2, 276 (1974). 10.1002/jss.400020219
19. L. Lerman, Proc. Natl. Acad. Sci. U.S.A. 68, 1886 (1971). 10.1073/pnas.68.8.1886
20. A. Zinchenko and K. Yoshikawa, Biophys. J. 88, 4118 (2005). 10.1529/biophysj.104.057323
21. U. Laemmli, Proc. Natl. Acad. Sci. U.S.A. 72, 4288 (1975). 10.1073/pnas.72.11.4288
22. D. Chattoraj, L. Gosule, and J. Schellman, J. Mol. Biol. 121, 327 (1978). 10.1016/0022-2836(78)90367-4
23. S. Mel'nikov, V. Sergeyev, and K. Yoshikawa, J. Am. Chem. Soc. 117, 2401 (1995). 10.1021/ja00114a004
24. S. Mel'nikov, V. Sergeyev, and K. Yoshikawa, J. Am. Chem. Soc. 117, 9951 (1995). 10.1021/ja00145a003
25. S. Dias, R. Mel'nikov, B. Lindman, and M. Miguel, Langmuir 16, 9577 (2000). 10.1021/la000640f
26. T. Yager, C. McMurray, and K. Van Holde, Biochemistry 28, 2271 (1989). 10.1021/bi00431a045
27. S. Mel'nikov, V. Sergeyev, K. Yoshikawa, H. Takahashi, and I. Hatta, J. Chem. Phys. 107, 6917 (1997). 10.1063/1.474932
28. M. Cao, M. Deng, X.-L. Wang, and Y. Wang, J. Phys. Chem. B 112, 13648 (2008). 10.1021/jp803244f
29. S. Kidoaki and K. Yoshikawa, Biophys. Chem. 76, 133 (1999). 10.1016/S0301-4622(98)00231-2
30. Y. Mel'nikova and B. Lindman, Langmuir 16, 5871 (2000). 10.1021/la991382t
31. M. Hays, C. Jewell, D. Lynn, and N. Abbott, Langmuir 23, 5609 (2007). 10.1021/la0700319
32. A.-L. Le Ny and C. Lee, J. Am. Chem. Soc. 128, 6400 (2006). 10.1021/ja0576738
33. A.-L. Le Ny and C. Lee, Biophys. Chem. 142, 76 (2009). 10.1016/j.bpc.2009.03.010
34. M. Sollogoub, S. Guieu, M. Geoffroy, A. Yamada, A. Estévez-Torres, K. Yoshikawa, and D. Baigl, ChemBioChem 9, 1201 (2008). 10.1002/cbic.200800072
35. M. Geoffroy, D. Faure, R. Oda, D. Bassani, and D. Baigl, ChemBioChem 9, 2382 (2008). 10.1002/cbic.200800235
36. A. Diguet, N. Mani, M. Geoffroy, M. Sollogoub, and D. Baigl, Chem. Eur. J. 16, 11890 (2010). 10.1002/chem.201001579
37. S. Rudiuk, K. Yoshikawaa, and D. Baigl, Soft Matter 7, 5854 (2011). 10.1039/c1sm05314k
38. A. Zinchenko, M. Tanahashi, and S. Murata, ChemBioChem 13, 105 (2012). 10.1002/cbic.201100492
39. Y. Zakrevskyy, A. Kopyshev, N. Lomadze, E. Morozova, L. Lysyakova, N. Kasyanenko, and S. Santer, Phys. Rev. E 84, 021909 (2011). 10.1103/PhysRevE.84.021909
40. Y. Zakrevskyy, J. Roxlau, G. Brezesinski, N. Lomadze, and S. Santer, J. Chem. Phys. 140, 044906 (2014). 10.1063/1.4862678
41. Y. Zakrevskyy, P. Cywinski, M. Cywinska, J. Paasche, N. Lomadze, O. Reich, H.-G. Löhmannsröben, and S. Santer, J. Chem. Phys. 140, 044907 (2014). 10.1063/1.4862679
42. A. Estèvez-Torres and D. Baigl, Soft Matter 7, 6746 (2011). 10.1039/c1sm05373f
43. D. Dumont, T. V. Galstian, S. Senkow, and A. M. Ritcey, Mol. Cryst. Liq. Cryst. 375, 341 (2002). 10.1080/10587250210555
44. Y. Zakrevskyy, M. Richter, S. Zakrevska, N. Lomadze, R. von Klitzing, and S. Santer, Adv. Funct. Mater. 22, 5000 (2012). 10.1002/adfm.201200617
45. A. Chatterjee, S. Moulik, S. Sanyal, B. Mishra, and P. Puri, J. Phys. Chem. B 105, 12823 (2001). 10.1021/jp0123029