journal article·2024-01-01Open access

Structures and Antibacterial Properties of DNA Ion Complex Films Consisting of Different Cationic Surfactants with the Same Carbon Number in Their Tails

Diaa Hamed Abdelshafy Abdelsalam, Rikako Yamakita, Takashi Aoki

Abstract

DNA ion complexes were prepared from DNA and two forms of cationic surfactants, hexadecylpyridinium chloride (HDPyCl) (also known as cetylpyridinium chloride (CPC)) and hexadecyltrimethylammonium bromide (HDTMABr) (also known as cetyltrimethylammonium bromide (CTAB)), which are antibacterial and have the same sixteen carbons in their tail alkyl chains, but different polar head groups. The anionic DNA and the cationic surfactant were sufficiently reacted and washed well to obtain DNA ion complexes with equal moles. These films were prepared using iso-propanol. The bulk and surface structure of the films were examined and compared using small angle X-ray scattering (SAXS), a gas pycnometer, attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), X-ray photoelectron spectroscopy (XPS), a static water contact angle meter, and atomic force microscopy (AFM). The two different DNA ion complex films consisting of surfactants with the same carbon number were found to be different in their DNA-DNA distances, film densities, and surface chemical compositions. Both films showed antibacterial properties.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Molecular Sensors and Ion Detection · Antimicrobial agents and applications · Biopolymer Synthesis and Applications

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

Affiliations

Department of Biobased Materials Science, Kyoto Institute of Technology

Faculty of Fiber Science and Engineering, Kyoto Institute of Technology

References (66)

Show source-provided references
1. A. Trewavas, Anal. Biochem., 21, 324 (1967).10.1016/0003-2697(67)90198-4 ↗
2. A. Sibatani, Anal. Biochem., 33, 279 (1970).10.1016/0003-2697(70)90298-8 ↗
3. V. D. Osica, T. L. Pyatigorskaya, O. F. Polyvtsev, A. T. Dembo, M. O. Kliya, V N. Vasilchenko, B. I. Verkin, and B. Y. Sukharevskya, Nucleic Acids Res., 4, 1083 (1977).10.1093/nar/4.4.1083 ↗
4. P. Geck, I. Nász, Anal Biochem., 135, 264 (1983).10.1016/0003-2697(83)90681-4 ↗
5. DNA Interactions with Polymers and Surfactants, ed. by R. Dias, B. Lindman, Wiley-Interscience, A John Wiley & Sons, Inc., (2007).
6. K. Tanaka and Y. Okahata, J. Am. Chem. Soc., 118, 10679 (1996).10.1021/ja9617855 ↗
7. H. Nakayama, H. Ohno, and Y. Okahata, Chem. Commun., 2300 (2001).10.1039/b107228e ↗
8. J. G. Grote, J. A. Hagen, J. S. Zetts, R. L. Nelson, D. E. Diggs, M. O. Stone, P. P. Yaney, E. Heckman, C. Zhang, W. H. Steier, A. K.-Y. Jen, L. R. Dalton, N. Ogata, M. J. Curley, S. J. Clarson, and F. K. Hopkins, J. Phys. Chem. B, 108, 8584 (2004).10.1021/jp038056d ↗
9. A. C. Brown and T. R. Fraser, Proc. Roy. Soc. Edinburgh, 6, 556 (1869).10.1017/S0370164600046186 ↗
10. B. F. Miller and Z. Baker, Science, 91, 624 (1940).10.1126/science.91.2374.624 ↗
11. M. R. Warren, T. J. Becker, D. G. Marsh, and R. S. Shelton, J. Pharmacol. Exp. Ther., 74, 401 (1942).
12. C. L. Huyck, Am. J. Pharm., 116, 50 (1944).
13. J. W. Nelson and S. C. Lyster, J. Am. Pharm. Assoc., 35, 89 (1946).10.1002/jps.3030350308 ↗
14. J. Witt, N. Ramji, R. Gibb, J. Dunavent, J. Flood, and J. Barnes, J. Contemp. Dent. Pract., 6, 1 (2005).10.5005/jcdp-6-1-1 ↗
15. S. Haps, D. E. Slot, C. E. Berchier, and G. A. Van der Weijden, Int. J. Dent. Hyg., 6, 290 (2008).10.1111/j.1601-5037.2008.00344.x ↗
16. R. Michael E. Richards, James Z. Xing, and Kirsty M. B. Mackay, Pharm. Res., 13, 1258 (1996).10.1023/A:1016084824877 ↗
17. M. Singh, V. S. Gill, H. Thippareddi, R. K. Phebus, J. L. Marsden, T. J. Herald, and A. L. Nutsch, J. Food Prot., 68, 1823 (2005).10.4315/0362-028X-68.9.1823 ↗
18. K. Lim and A. Mustapha, Food Microbiol., 24, 89 (2007).10.1016/j.fm.2006.04.005 ↗
19. K. Matsuo, K. Yoshihara, N. Nagaoka, Y. Makita, H. Obika, T. Okihara, A. Matsukawa, Y. Yoshida, and B. V. Meerbeek, Acta Biomater., 100, 388 (2019).10.1016/j.actbio.2019.09.045 ↗
20. C. G. Densmore, T. W. Robison, B. F. Smith, and R. E. Lewis, J. Appl. Polym Sci., 99, 3153 (2006).10.1002/app.23210 ↗
21. H. Kitagawa, K. Takeda, R. Kitagawa, N. Izutani, S. Miki, N. Hirose, M. Hayashi, and S. Imazato, Acta Biomater., 10, 4285 (2014).10.1016/j.actbio.2014.06.016 ↗
22. D. L. Popkin, S. Zilka, M. Dimaano, H. Fujioka, C. Rackley, R. Salata, A. Griffith, P. K. Mukherjee, M. A. Ghannoum, and F. Esper, Pathogens and Immunity, 2, 253 (2017).10.20411/pai.v2i2.200 ↗
23. P. H. Sette-de-Souza, J. C. Soares Martins, A. V. Martins-de-Barros, B Rodrigues Vieira, M. J. Fernandes Costa, and F. A. da Costa Araújo, Eur. Rev. Med. Pharmacol. Sci., 24, 10222 (2020).
24. F. Carrouel, L. S. Gonçalves, M. P. Conte, G. Campus, J. Fisher, L. Fraticelli1, E. Gadea-Deschamps, L. Ottolenghi, and D. Bourgeois, J. Dent. Res., 100, 124 (2021).10.1177/0022034520967933 ↗
25. M. Bañó-Polo, L. Martínez-Gil, M. M. S. del Pino, A. Massoli, I. Mingarro, R. Léon and M. Jesus Garcia-Murria, J. Oral Microbiol., 14, 2030094, (2022).10.1080/20002297.2022.2030094 ↗
26. R. Takeda, H. Sawa, M. Sasaki, Y. Orba, N. Maishi, T. Tsumita, N. Ushijima, Y. Hida, H. Sano, Y. Kitagawa, K. Hida, Sci. Rep., 12, 14050 (2022).10.1038/s41598-022-18367-6 ↗
27. W. G. Salt and D. Wiseman, J. Pharm. Pharmacol., 22, 261 (1970).10.1111/j.2042-7158.1970.tb08516.x ↗
28. J. A. Sands, FEMS Microbiol. Lett., 36, 261 (1986).10.1016/0378-1097(86)90323-X ↗
29. R. F. Itzhaki, Biochem. J., 122, 583 (1971).10.1042/bj1220583 ↗
30. A. Schaper, J. P. P. Starink, and T. M. Jovin, FEBS Lett., 355, 91 (1994).10.1016/0014-5793(94)01166-4 ↗
31. L. Wang, J. Yoshida, N. Ogata, S. Sasaki, and T. Kajiyama, Chem. Mater., 13, 1273 (2001).10.1021/cm000869g ↗
32. A. Radko, S. Lalik, A. Deptuch, T. Jaworska-Gołąb, R. Ekiert, N. Górska, K. Makyła-Juzak, J. Nizioł, and M. Marzec, Polymer, 235, 124277 (2021).10.1016/j.polymer.2021.124277 ↗
33. S. M. Mel’nikov, V. G. Sergeyev, and K. Yoshikawa, J. Am. Chem. Soc., 117, 2401 (1995).10.1021/ja00114a004 ↗
34. V. G. Sergeyev, S. V. Mikhailenko, O. A. Pyshkina, I. V. Yaminsky, and K. Yoshikawa, J. Am. Chem. Soc., 121, 1780 (1999).10.1021/ja981683+ ↗
35. D. H. A. Abdelsalam and T. Aoki, J. Fiber Sci. and Tech., 79, 250 (2023).10.2115/fiberst.2023-0027 ↗
36. S. K. Mehta, S. Kumar, S. Chaudhary, and K. K. Bhasin, Nanoscale Res. Lett., 4, 1197 (2009).10.1007/s11671-009-9377-8 ↗
37. P. T. Jacobs, and E. W. Anacker, J. Colloid Interface Sci., 44, 505 (1973).10.1016/0021-9797(73)90328-7 ↗
38. R. Ghirlando, E. J. Wachtel, T. Arad, and A. Minsky, Biochemistry, 31, 7110 (1992).10.1021/bi00146a012 ↗
39. J. O. Rädler, I. Koltover, T. Salditt, and C. R. Safinya, Science, 275, 810 (1997).10.1126/science.275.5301.810 ↗
40. T. Pfohl, Y. Li, J. H. Kim, Z. Wen, G. C. L. Wong, I. Koltover, M. W. Kim, and C. R. Safinya, Colloids and Surfaces A: Physicochem. Eng. Aspects, 198-200, 613 (2002).10.1016/S0927-7757(01)00978-5 ↗
41. K. D. Danov, E. S. Basheva, P. A. Kralchevsky, K. P. Ananthapadmanabhan, and A. Lips, Adv. Colloid Interface Sci., 168, 50 (2011).10.1016/j.cis.2011.03.006 ↗
42. S. E. Anachkov, K. D. Danov, E. S. Basheva, P. A. Kralchevsky, and K. P. Ananthapadmanabhan, Adv. Colloid Interface Sci., 183-184, 55 (2012).10.1016/j.cis.2012.08.003 ↗
43. J. Tabony, Mol. Phys., 51, 975 (1984).10.1080/00268978400100641 ↗
44. R. A. Robinson and R. H. Stokes, p. 124, Electrolyte Solutions, Butterworth, London (1970).
45. H. H. Paradies and F. Habben, Acta Cryst., C49, 744 (1993).10.1107/S010827019201179X ↗
46. S. G. Slade, M. Raupach, and W. W. Emerson, Clays Clay Miner., 26, 125 (1978).10.1346/CCMN.1978.0260207 ↗
47. J. Bors, Á. Patzkób, and I. Dékány, Appl. Clay Sci., 19, 27 (2001).10.1016/S0169-1317(01)00060-6 ↗
48. R. Chitrakar, Y. Makita, A. Sonoda, and T. Hirotsu, Appl. Clay Sci., 51, 375 (2011).10.1016/j.clay.2010.11.033 ↗
49. W. T. Astbury, Symp. Soc. Exp. Biol., 1, 66 (1947).
50. R. E. Franklin and R. G. Gosling, Acta Crystallogr., 6, 678 (1953).10.1107/S0365110X53001940 ↗
51. T. Weidlich, S. M. Lindsay, A. Rupprecht, Biopolymers, 26, 439 (1987).10.1002/bip.360260310 ↗
52. E. F. Cooper and A. F. A. Asfour, J. Chem. Eng. Data, 36, 285 (1991).10.1021/je00003a008 ↗
53. R. G. Snyder, S. L. Hsu, and S. Krimm, Spectrochimica Acta Part A: Molecular Spectroscopy, 34, 395 (1978).10.1016/0584-8539(78)80167-6 ↗
54. T. Kawai, J. Umemura, and T. Takenaka, Bull. Inst. Chem. Res., Kyoto Univ., 61, 314 (1983).
55. D. Chapman, Chem. Rev., 62, 433 (1962).10.1021/cr60219a003 ↗
56. Y. Koyama, M. Yanagishita, S. Toda, and T Matsuo, J. Colloid Interface Sci., 61, 438 (1977).10.1016/0021-9797(77)90462-3 ↗
57. D. G. Cameron, H. L. Casal, E. F. Gudgin, and H. H. Mantsch, Biochim. Biophys. Acta - Biomembranes, 596, 463 (1980).10.1016/0005-2736(80)90135-2 ↗
58. Z. Li, W.-T. Jiang and H. Hong, Spectrochim. Acta Part A: Molecular and Biomolecular Spectroscopy, 71, 1525 (2008).10.1016/j.saa.2008.05.015 ↗
59. T. Kawai, J. Umemura, T. Takenaka, M. Kodama, Y. Ogawa, and S. Seki, Langmuir, 2, 739 (1986).10.1021/la00072a011 ↗
60. D. R. Scheuing and J. G. Weers, Langmuir, 6, 665 (1990).10.1021/la00093a023 ↗
61. T. C. Wong, N. B. Wong, and P. A. Tanner, J. Colloid Interface Sci., 186, 325 (1997).10.1006/jcis.1996.4674 ↗
62. T. Kobayashi, K. Mao, S.-G. Wang, V. S.-Y. Lin, and M. Pruski, Solid State Nucl. Magn. Reson., 39, 65 (2011).10.1016/j.ssnmr.2011.02.001 ↗
63. C.-Y. Lee, P. Gong, G. M. Harbers, D. W. Grainger, D. G. Castner, and L. J. Gamble, Anal. Chem., 78, 3316 (2006).10.1021/ac052137j ↗
64. M. R. Vilar, A. M. B. do Rego, A. M. Ferraria, Y. Jugnet, C. Noguès, D. Peled, and R. Naaman, J. Phys. Chem. B, 112, 6957 (2008).10.1021/jp8008207 ↗
65. S. Ardizzone, C. L. Bianchi, and G. Cappelletti, Surf. Interface Anal., 38, 452 (2006).10.1002/sia.2196 ↗
66. A. R. Bucci, L. Marcelino, R. K. Mendes, and A. Etchegaray, World J. Microbiol. Biotechnol., 34, 86 (2018).10.1007/s11274-018-2472-1 ↗