Midinfrared surface-plasmon resonance: A novel biophysical tool for studying living cells

Journal of Applied Physics

Volumn 105, Issue 10, 2009, Pages

  Golosovsky, M ^a   Lirtsman, V ^a   Yashunsky, V ^a   Davidov, D ^a   Aroeti, B ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AQUEOUS SOLUTIONS; BIOLOGICAL STUDIES; CLATHRIN; D-GLUCOSE; FOURIER TRANSFORM INFRARED SPECTROMETRY; FTIR; INFRARED RANGE; LIVING CELL; MIDINFRARED; PLASMA MEMBRANES; SURFACE PLASMON TECHNIQUES; VISIBLE RANGE;

CELL CULTURE; CELL MEMBRANES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GLUCOSE; PLASMONS; SUSPENSIONS (FLUIDS);

SURFACE PLASMON RESONANCE;

EID: 66549120183     PISSN: 00218979     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3116143     Document Type: Article

References (56)

1. H. Raether, Surface plasmons on smooth and rough surfaces and on coatings (Springer, Berlin, 1988).
2. S. A. Maier, Plasmonics: Applications and Fundamentals (Springer, New York, 2007).
3. W. Knoll, Annu. Rev. Phys. Chem. 0066-426X 49, 569 (1998). 10.1146/annurev.physchem.49.1.569
4. S. A. Maier and H. A. Atwater, J. Appl. Phys. 0021-8979 98, 011101 (2005). 10.1063/1.1951057
5. G. Gauglitz, G. Proll, Biosensing for the 21 century 109, 395 (2008). 10.1007/10-2007-076 0021-8979
6. J. Homola, S. S. Yee, and G. Gauglitz, Sens. Actuators B 0925-4005 54, 3 (1999). 10.1016/S0925-4005(98)00321-9
7. J. Homola, Anal. Bioanal. Chem. 1618-2642 377, 528 (2003). 10.1007/s00216-003-2101-0
8. J. Homola, Chem. Rev. (Washington, D.C.) 0009-2665 108, 462 (2008). 10.1021/cr068107d
9. K. S. Phillips and Q. Cheng, Anal. Bioanal. Chem. 1618-2642 387, 1831 (2007). 10.1007/s00216-006-1052-7
10. R. L. Rich and D. G. Myszka, Curr. Opin. Biotechnol. 0958-1669 11, 54 (2000). 10.1016/S0958-1669(99)00054-3
11. A. J. Haes and R. P. Van Duyne, Anal. Bioanal. Chem. 1618-2642 379, 920 (2004). 10.1007/s00216-004-2708-9
12. R. Ince and R. Narayanaswamy, Anal. Chim. Acta 0003-2670 569, 1 (2006). 10.1016/j.aca.2006.03.058
13. X. D. Hoa, A. G. Kirk, and M. Tabrizian, Biosens. Bioelectron. 0956-5663 23, 151 (2007). 10.1016/j.bios.2007.07.001
14. R. J. Green, R. A. Frazier, K. M. Shakeshe, M. C. Davies, C. J. Roberts, and S. J. B. Tendler, Biomaterials 0142-9612 21, 1823 (2000). 10.1016/S0142-9612(00)00077-6
15. I. D. Alves, C. K. Park, and V. J. Hruby, Curr. Protein Pept. Sci. 1389-2037 6, 293 (2005). 10.2174/1389203054546352
16. M. Besenicar, P. Macek, J. H. Lakey, and G. Anderluh, Chem. Phys. Lipids 0009-3084 141, 169 (2006). 10.1016/j.chemphyslip.2006.02.010
17. A. Dahlin, M. Zach, T. Rindzevicius, M. Kall, D. S. Sutherland, and F. Hook, J. Am. Chem. Soc. 0002-7863 127, 5043 (2005). 10.1021/ja043672o
18. P. Pattnaik, Appl. Biochem. Biotechnol. 0273-2289 126, 79 (2005). 10.1385/ABAB:126:2:079
19. Z. Salamon, H. A. Macleod, and G. Tollin, Biochim. Biophys. Acta 0006-3002 1331, 117 (1997).
20. Z. Salamon, G. Lindblom, and G. Tollin, Biophys. J. 0006-3495 84, 1796 (2003). 10.1016/S0006-3495(03)74987-X
21. M. P. Jonsson, P. Jonsson, A. B. Dahlin, and F. Hook, Nano Lett. 1530-6984 7, 3462 (2007). 10.1021/nl072006t
22. K. Morigaki and K. Tawa, Biophys. J. 0006-3495 91, 1380 (2006). 10.1529/biophysj.106.086074
23. Y. Fang, A. M. Ferrie, N. H. Fontaine, J. Mauro, and J. Balakrishnan, Biophys. J. 0006-3495 91, 1925 (2006). 10.1529/biophysj.105.077818
24. K. F. Giebel, C. Bechinger, S. Herminghaus, M. Riedel, P. Leiderer, U. Weiland, and M. Bastmeyer, Biophys. J. 0006-3495 76, 509 (1999). 10.1016/S0006-3495(99)77219-X
25. M. Hide, T. Tsutsui, H. Sato, T. Nishimura, K. Morimoto, S. Yamamoto, and K. Yoshizato, Anal. Biochem. 0003-2697 302, 28 (2002). 10.1006/abio.2001.5535
26. Y. Yanase, H. Suzuki, T. Tsutsui, I. Uechi, T. Hiragun, S. Mihara, and M. Hide, Biosens. Bioelectron. 0956-5663 22, 1081 (2007). 10.1016/j.bios.2006.03. 011
27. T. Liebermann and W. Knoll, Colloids Surf., A 0927-7757 171, 115 (2000). 10.1016/S0927-7757(99)00550-6
28. J. M. Brockman, B. P. Nelson, and R. M. Corn, Annu. Rev. Phys. Chem. 0066-426X 51, 41 (2000). 10.1146/annurev.physchem.51.1.41
29. A. A. Kolomenskii, P. D. Gershon, and H. A. Schuessler, Appl. Opt. 0003-6935 39, 3314 (2000). 10.1364/AO.39.003314
30. M. Zangeneh, N. Doan, E. Sambriski, and R. H. Terrill, Appl. Spectrosc. 0003-7028 58, 10 (2004). 10.1366/000370204322729414
31. Z. -M. Qi, M. Wei, H. Matsuda, I. Honma, and H. Zhou, Appl. Phys. Lett. 0003-6951 90, 181112 (2007). 10.1063/1.2734898
32. J. V. Coe, K. R. Rodriguez, S. Teeters-Kennedy, K. Cilwa, J. Heer, H. Tian, and S. M. Williams, J. Phys. Chem. 0022-3654 111, 17459 (2007).
33. G. Brink, H. Sigl, and E. Sackmann, Sens. Actuators B 0925-4005 25, 756 (1995). 10.1016/0925-4005(95)85168-2
34. A. Ikehata, X. L. Li, T. Itoh, Y. Ozaki, and J. H. Jiang, Appl. Phys. Lett. 0003-6951 83, 2232 (2003). 10.1063/1.1610812
35. A. Ikehata, T. Itoh, and Y. Ozaki, Anal. Chem. 0003-2700 76, 6461 (2004). 10.1021/ac049003a
36. J. F. Masson, Y. C. Kim, A. Loius, L. A. Obando, W. Peng, and K. S. Booksch, Appl. Spectrosc. 0003-7028 60, 1241 (2006).
37. S. Patskovsky, A. V. Kabashin, M. Meunier, and J. H. T. Luong, J. Opt. Soc. Am. A Opt. Image Sci. Vis. 20, 1644 (2003). 10.1364/JOSAA.20.001644 1084-7529
38. S. Patskovsky, A. V. Kabashin, M. Meunier, and J. H. T. Luong, Sens. Actuators B 0925-4005 97, 409 (2004). 10.1016/j.snb.2003.09.023
39. A. G. Frutos, S. C. Weibel, and R. M. Corn, Anal. Chem. 0003-2700 71, 3935 (1999). 10.1021/ac9905165
40. B. P. Nelson, A. G. Frutos, J. M. Brockman, and R. M. Corn, Anal. Chem. 0003-2700 71, 3928 (1999). 10.1021/ac990517x
41. V. Lirtsman, R. Ziblat, M. Golosovsky, D. Davidov, R. Pogreb, V. Sacks-Granek, and J. Rishpon, J. Appl. Phys. 0021-8979 98, 093506 (2005). 10.1063/1.2123370
42. R. Ziblat, V. Lirtsman, D. Davidov, and B. Aroeti, Biophys. J. 0006-3495 90, 2592 (2006). 10.1529/biophysj.106.0900139
43. V. Lirtsman, M. Golosovsky, and D. Davidov, J. Appl. Phys. 0021-8979 103, 014702 (2008). 10.1063/1.2828162
44. V. Yashunsky, S. Shimron, V. Lirtsman, A. M. Weiss, N. Melamed-Book, M. Golosovsky, D. Davidov, and B. Aroeti, Biophys. J. 0006-3495 (unpublished).
45. K. Johansen, H. Arwin, I. Lundstrom, and B. Liedberg, Rev. Sci. Instrum. 0034-6748 71, 3530 (2000). 10.1063/1.1287631
46. G. W. Bradberry and J. R. Sambles, Opt. Commun. 0030-4018 67, 404 (1988). 10.1016/0030-4018(88)90209-X
47. W. W. Lam, L. H. Chu, and C. L. Wong, Sens. Actuators B 0925-4005 105, 138 (2005). 10.1016/j.snb.2004.04.088
48. K. Aslan, J. R. Lakowicz, and C. D. Geddes, Anal. Chem. 0003-2700 77, 2007 (2005). 10.1021/ac0484880
49. H. V. Hsieh, Z. A. Pfeiffer, T. J. Amiss, D. B. Sherman, and J. Bruce Pitner, Biosens. Bioelectron. 0956-5663 19, 653 (2004). 10.1016/S0956-5663(03) 00271-9
50. E. D. Palik, Handbook of Optical Constants of Solids II (Academic, New York, 1991).
51. The phosphate-buffered saline buffer (PBS) has a pH of 7.4 and contains 137 nM NaCl, 8.9 mM Na2 HPO4, 2.7 mM KCl, 1.5 mM KH2 PO4. We used (from healthy donors) fresh human erythrocytes that were washed in PBS and centrifugated three times for 5 min at 300×g. The washed erythrocytes were suspended in the PBS and stored in ice.
52. Y. Hayashi, L. Lifshitz, A. Caduff, and Y. Feldman, J. Phys. D 0022-3727 36, 369 (2003). 10.1088/0022-3727/36/4/307
53. A. Yariv and P. Yeh, Optical Waves in Crystals (Wiley, New York, 1984), p. 473.
54. M. P. Besenicar, A. Bavdek, A. Kladnik, P. Macek, and G. Anderluh, Biochim. Biophys. Acta 0006-3002 1778, 175 (2008). 10.1016/j.bbamem.2007.09.022
55. The cells were imaged with an Olympus FV-1000 confocal microscope, equipped with an on-scope incubator (Life Image Services). The holo-Ft was tagged with rhodamine red.
56. K. K. Chittur, Biomaterials 0142-9612 19, 357 (1998). 10.1016/S0142-9612(97)00223-8