journal article·2012-01-24

Ferritin-Based New Magnetic Force Microscopic Probe Detecting 10 nm Sized Magnetic Nanoparticles

Duckhoe Kim, Nak-Kwan Chung, Stephanie Allen, Saul J. B. Tendler, Joon Won Park

ACS Nano· Volume 6· Issue 1
Publisher page

Abstract

A single-molecule ferritin picking-up process was realized with the use of AFM, which was enhanced by employing controlled dendron surface chemistry. The approach enabled the placement of a single ferritin protein molecule at the very end of an AFM tip. When used for magnetic force microscopy (MFM) imaging, the tips were able to detect magnetic interactions of approximately 10 nm sized magnetic nanoparticles. The single ferritin tip also showed the characteristics of a "multifunctional" MFM probe that can sense the magnetic force from magnetic materials as well as detect the biomolecular interaction force with DNAs on the surface. The multifunctional tip enabled us not only to investigate the specific molecular interaction but also to image the magnetic interaction between the probe and the substrate, in addition to allowing the common capability of topographic imaging. Because the protein engineering of ferritin and the supporting coordination and conjugation chemistry are well-established, we envisage that it would be straightforward to extend this approach to the development of various single magnetic particle MFM probes of different compositions and sizes.
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Research context

OpenAlex topics: Force Microscopy Techniques and Applications · Advanced biosensing and bioanalysis techniques · Molecular Junctions and Nanostructures

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

Affiliations

Department of Chemistry, Pohang University of Science and Technology, San 31, Hyoja-dong, Pohang, Korea

Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, United Kingdom

Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, San 31, Hyoja-dong, Pohang, Korea.

References (52)

Show source-provided references
1. Sun S. · J. Appl. Phys. · 1999 · 85 · 432510.1063/1.370357 ↗
2. Sun S. · Science · 2000 · 287 · 198910.1126/science.287.5460.1989 ↗
3. Kiselev S. I. · Nature · 2003 · 425 · 38010.1038/nature01967 ↗
4. Puntes V. F. · Appl. Phys. Lett. · 2001 · 78 · 218710.1063/1.1362333 ↗
5. Puntes V. F. · Nat. Mater. · 2004 · 3 · 26310.1038/nmat1094 ↗
6. Song E. Q. · ACS Nano · 2011 · 5 · 76110.1021/nn1011336 ↗
7. Wittrup A. · Proc. Natl. Acad. Sci. U.S.A. · 2010 · 107 · 1334210.1073/pnas.1002622107 ↗
8. Martinez-Morales A. A. · Adv. Mater. · 2008 · 20 · 481610.1002/adma.200702863 ↗
9. Moskalenko A. V. · Biophys. J. · 2010 · 98 · 47810.1016/j.bpj.2009.10.021 ↗
10. Liong M. · ACS Nano · 2008 · 2 · 88910.1021/nn800072t ↗
11. Wang Y. · Adv. Funct. Mater. · 2008 · 18 · 30810.1002/adfm.200700456 ↗
12. Hill H. D. · Anal. Chem. · 2007 · 79 · 921810.1021/ac701626y ↗
13. Sedman V. L. · J. Am. Chem. Soc. · 2006 · 128 · 690310.1021/ja060358g ↗
14. Blunt M. O. · Nat. Nanotechnol. · 2007 · 2 · 16710.1038/nnano.2007.25 ↗
15. Hill R. J. A. · Adv. Mater. · 2007 · 19 · 447410.1002/adma.200700590 ↗
16. Sahin O. · Nat. Nanotechnol. · 2007 · 2 · 50710.1038/nnano.2007.226 ↗
17. Husale S. · Nature · 2009 · 462 · 107510.1038/nature08626 ↗
18. Hinterdorfer P. · Nat. Methods · 2006 · 3 · 34710.1038/nmeth871 ↗
19. Struckmeier J. · Nanotechnology · 2008 · 19 · 38402010.1088/0957-4484/19/38/384020 ↗
20. Müller D. J. · Curr. Biol. · 2011 · 21 · R21210.1016/j.cub.2011.01.046 ↗
21. Martin Y. · Appl. Phys. Lett. · 1987 · 50 · 145510.1063/1.97800 ↗
22. Giles R. · Appl. Phys. Lett. · 1993 · 63 · 61710.1063/1.109967 ↗
23. Rasa M. · J. Colloid Interface Sci. · 2002 · 250 · 30310.1006/jcis.2002.8345 ↗
24. Schreiber S. · Small · 2008 · 4 · 27010.1002/smll.200700116 ↗
25. Deng Z. · Appl. Phys. Lett. · 2004 · 85 · 626310.1063/1.1842374 ↗
26. Dietz C. · Nanotechnology · 2011 · 22 · 12570810.1088/0957-4484/22/12/125708 ↗
27. Li J. W. · Appl. Phys. Lett. · 2009 · 94 · 16311810.1063/1.3126521 ↗
28. Neves C. S. · Nanotechnology · 2010 · 21 · 30570610.1088/0957-4484/21/30/305706 ↗
29. Chasteen N. D. · J. Struct. Biol. · 1999 · 126 · 18210.1006/jsbi.1999.4118 ↗
30. Liu X. · Acc. Chem. Res. · 2005 · 38 · 16710.1021/ar0302336 ↗
31. Gálvez N. · J. Am. Chem. Soc. · 2008 · 130 · 806210.1021/ja800492z ↗
32. Gálvez N. · J. Mater. Chem. · 2006 · 16 · 275710.1039/B604860A ↗
33. Shin Y. · J. Phys. Chem. C · 2010 · 114 · 598510.1021/jp911004a ↗
34. Zhang L. · Nano Lett. · 2010 · 10 · 21910.1021/nl903313r ↗
35. Gálvez N. · Inorg. Chem. · 2010 · 49 · 170510.1021/ic902128g ↗
36. Douglas T. · Inorg. Chem. · 2000 · 39 · 182810.1021/ic991269q ↗
37. Kim J. W. · Chem. Commun. · 2005 · 410110.1039/b505097a ↗
38. Hennequin B. · Adv. Mater. · 2008 · 20 · 359210.1002/adma.200800530 ↗
39. Fernández B. · Adv. Funct. Mater. · 2008 · 18 · 393110.1002/adfm.200800942 ↗
40. Kufer S. K. · Science · 2008 · 319 · 59410.1126/science.1151424 ↗
41. Liu N. · J. Am. Chem. Soc. · 2010 · 132 · 1103610.1021/ja1052544 ↗
42. Liu K. · J. Am. Chem. Soc. · 2011 · 133 · 322610.1021/ja108022h ↗
43. Kim D. · Soft Matter · 2010 · 6 · 397910.1039/c001722a ↗
44. Jung Y. J. · J. Am. Chem. Soc. · 2007 · 129 · 934910.1021/ja0676105 ↗
45. Roy D. · Anal. Chem. · 2010 · 82 · 518910.1021/ac100476b ↗
46. Kim I. H. · Anal. Chem. · 2009 · 81 · 327610.1021/ac8024366 ↗
47. Jung Y. J. · Nucleic Acids Res. · 2009 · 37 · e1010.1093/nar/gkn965 ↗
48. Kim J. S. · Adv. Mater. · 2009 · 21 · 78610.1002/adma.200801323 ↗
49. Florin E. L. · Science · 1994 · 264 · 41510.1126/science.8153628 ↗
50. Lo Y. S. · Langmuir · 1999 · 15 · 137310.1021/la981003g ↗
51. Nikitenko S. I. · J. Phys. Chem. B · 2004 · 108 · 762010.1021/jp036376r ↗
52. Tsang S. C. · Chem. Phys. Lett. · 2000 · 322 · 55310.1016/S0009-2614(00)00470-X ↗