Biotinylated lipid membrane patterns supported by proteins for the recognition of streptavidined polystyrene microspheres

Journal of Nanoscience and Nanotechnology

Volumn 10, Issue 10, 2010, Pages 6318-6323

  Hua, Deyao ^a   Yang, Yang ^b   Zhang, Xiaoming ^a   Zhu, Pengli ^a   Fei, Jinbo ^a   Li, Junbai ^a,b  

^a PEKING UNIVERSITY   (China)

^b NATIONAL CENTER FOR NANOSCIENCE AND TECHNOLOGY   (China)

Author keywords

Lipid membrane; Molecular recognition; Pattern; Surface modification

Indexed keywords

BIOLOGICAL INTERFACE; FUNCTIONALIZED; GLASS SUBSTRATES; GOOD STABILITY; HIGH EFFICIENCY; HUMAN SERUM ALBUMINS; LIPID MEMBRANES; MICRO CONTACT PRINTING; PATTERN; PHOSPHOLIPIDS MEMBRANES; POLYSTYRENE MICRO-SPHERE; STREPTAVIDIN; SURFACE MODIFICATION;

BIOCHEMISTRY; BIOSENSORS; MICROSPHERES; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; PHOSPHOLIPIDS; POLYSTYRENES; SUBSTRATES; SURFACE CHEMISTRY;

MEMBRANES;

BIOTIN; GLASS; LIPOSOME; MICROSPHERE; PHOSPHOLIPID; POLYSTYRENE DERIVATIVE; SERUM ALBUMIN; STREPTAVIDIN;

ARTICLE; CHEMISTRY; HUMAN; METABOLISM; METHODOLOGY; MICROTECHNOLOGY; PARTICLE SIZE; SCANNING ELECTRON MICROSCOPY; SPECTROFLUOROMETRY;

BIOTIN; GLASS; HUMANS; LIPOSOMES; MICROSCOPY, ELECTRON, SCANNING; MICROSPHERES; MICROTECHNOLOGY; PARTICLE SIZE; PHOSPHOLIPIDS; POLYSTYRENES; SERUM ALBUMIN; SPECTROMETRY, FLUORESCENCE; STREPTAVIDIN;

EID: 79952200440     PISSN: 15334880     EISSN: None     Source Type: Journal    
DOI: 10.1166/jnn.2010.2527     Document Type: Article

References (29)

1. P. Vadgama, Annu. Rep. Prog. Chem., Sect. C 101, 14 (2005).
2. B. Kasemo, Surf. Sci. 500, 656 (2002).
3. E. Sackman, Science 271, 43 (1996).
4. M. Tanaka and E. Sackmann, Nature 437, 656 (2005).
5. S. Mitragotri and J. Lahann, Nature Materials 8, 15 (2009).
6. S. G. Zhang, L. Yan, M. Altman, M. Lassie, H. Nugent, F. Frankel, D. A. Lauffenburger, G. M. Whitesides, and A. Rich, Biomaterials 20, 1213 (1999).
7. D. Stamou, C. Duschl, E. Delamarche, and H. Vogel, Angew. Chem. Int. Ed. 42, 5580 (2003).
8. P. S. Cremer and S. G. Boxer, J. Phys. Chem. B 103, 2554 (1999).
9. T. Viitala, I. Vikholm, and J. Peltonen, Langmuir 16, 4953 (2000).
10. E. E. Ross, B. Bondurant, T. Spratt, J. C. Conboy, D. F. O'Brien, and S. S. Saavedra, Langmuir 17, 2305 (2001).
11. A. T. A. Jenkins, J. Hu, Y. Z. Wang, S. Schiller, R. Foerch, and W. Knoll, Langmuir 16, 6381 (2000).
12. Y. Fang, A. G. Frutos, and J. Lahiri, J. Am. Chem. Soc. 124, 2394 (2002).
13. L. Y. Hwang, H. Gotz, W. Knoll, C. J. Hawker, and C. W. Frank, Langmuir 24, 14088 (2008).
14. B. P. Oberts and G. J. Blanchard, Langmuir 25, 2962 (2009).
15. I. K. Vockenroth, P. P. Atanasova, A. T. A. Jenkins, and I. Köper, Langmuir 24, 496 (2008).
16. T. Ide, T. Kobayashi, and M. Hirano, Anal. Chem. 80, 7792 (2008).
17. M. P. Jonsson, P. Jönsson, A. B. Dahlin, and F. Höök, Nano Lett. 7, 3462 (2007).
18. R. N. Orth, T. G. Clark, and H. G. Craighead, Biomed. Microdevices 5, 29 (2003).
19. S. F. Fenz, R. Merkel, and K. Sengupta, Langmuir 25, 1074 (2009).
20. Y. K. Jung, T. W. Kim, C. Jung, D. Y Cho, and H. G. Park, Small 4, 1778 (2008).
21. Y. I. Katsura, T. Wazawa, T. Ban, K. Morigaki, and S. Aoyama, J. Biosci. Bioeng. 105, 527 (2008).
22. K. Ariga, J. P. Hill, M. V. Lee, A. Vinu, R. Charvet, and S. Acharya, Sci. Technol. Adv. Mater. 9, 014109 (2008).
23. J. R. Olivieri and A. F. Craievich, Eur. Biophys. J. 24, 77 (1995).
24. X. M. He and D. C. Carter, Nature 358, 209 (1992).
25. B. Wang, J. Feng, and C. Gao, Macromol. Biosci. 5, 767 (2005).
26. S. R. Clark, P. Billsten, and H. Elwing, Colloids Surf. B 2, 457 (1994).
27. X. M. Zhang, Q. He, Y. Cui, L. Duan, and J. B. Li, Biochem. Biophys. Res. Commun. 349, 920 (2006).
28. D. Kohlheyer, J. C. T. Eijkel, S. Schlautmann, A. V. D. Berg, and R. B. M. Schasfoort, Anal. Chem. 79, 8190 (2007).
29. F. M. Marassi, S. Djukic, and P. M. Macdonald, Biochem. Biophys. Acta Biomembr. 1146, 219 (1993).