journal article·2009-10-27

Interaction Forces and Reversible Collapse of a Polymer Brush-Gated Nanopore

Roderick Y. H. Lim, Jie Deng

ACS Nano· Volume 3· Issue 10
Publisher page

Abstract

Nanopores are ubiquitous in nature and technology, yet relatively little is known about how surface-grafted polymers can affect the interaction forces at the pore. By fabricating Au nanorings on Si substrates, we have constructed a unique experimental platform that allows for direct atomic force microscope (AFM) measurements to be made on polyethylene glycol (PEG) chains locally anchored onto a geometric pore surface. Force measurements show that the PEG gives rise to a steric repulsive barrier that envelops the entire nanoring, signifying polymer brush formation. This is confirmed by a direct imaging of the PEG brush, which reversibly collapses by switching between poor and good solvent conditions to "open" and "close" the pore, respectively. From the view of interaction forces, these results highlight possible functionalities in which polymer brushes may play a role in minimizing fouling/clogging effects in synthetic nanopores and biological nuclear pore complexes (NPCs). By the mechanism of a reversible collapse, this work illustrates how polymer brush-gated nanopores may be used as nonfouling sieves for small molecules and/or solvent-controlled chemical valves that regulate solute traffic.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Nanopore and Nanochannel Transport Studies · Polymer Surface Interaction Studies · Force Microscopy Techniques and Applications

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

Affiliations

Biozentrum and the Swiss Nanoscience Institute, University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland

Institute of Materials Research and Engineering, A*STAR (Agency for Science, Technology and Research), 3 Research Link, Singapore 117602

References (52)

Show source-provided references
1. Granick S. · J. Polym. Sci., Part B: Polym. Phys. · 2003 · 41 · 275510.1002/polb.10669 ↗
2. Langer R. · Nature · 1998 · 392 · 5
3. Bazile D. · J. Pharm. Sci. · 1995 · 84 · 49310.1002/jps.2600840420 ↗
4. Harris J. M. · Nat. Rev. Drug Discovery · 2003 · 2 · 21410.1038/nrd1033 ↗
5. Elbert D. L. · Annu. Rev. Mater. Sci. · 1996 · 26 · 36510.1146/annurev.ms.26.080196.002053 ↗
6. Harris J. M. · 199210.1007/978-1-4899-0703-5 ↗
7. Leckband D. · J. Biomater. Sci., Polym. Ed. · 1999 · 10 · 112510.1163/156856299X00720 ↗
8. Shannon M. A. · Nature · 2008 · 452 · 30110.1038/nature06599 ↗
9. Ito Y. · J. Am. Chem. Soc. · 1997 · 119 · 161910.1021/ja963418z ↗
10. Ito Y. · Langmuir · 2000 · 16 · 537610.1021/la991102+ ↗
11. Iwata H. · Macromolecules · 1998 · 31 · 367110.1021/ma971243n ↗
12. Mika A. M. · J. Membr. Sci. · 1999 · 153 · 4510.1016/S0376-7388(98)00246-4 ↗
13. Caspi Y. · Nano Lett. · 2008 · 8 · 372810.1021/nl801975q ↗
14. Jovanovic-Talisman T. · Nature · 2009 · 457 · 102310.1038/nature07600 ↗
15. Israelachvili J. N. · 1995
16. Butt H. J. · Surf. Sci. Rep. · 2005 · 59 · 110.1016/j.surfrep.2005.08.003 ↗
17. Ducker R. · Soft Matter · 2008 · 4 · 177410.1039/b804861b ↗
18. Jonas A. M. · Nano Lett. · 2008 · 8 · 381910.1021/nl802152q ↗
19. Jonas A. M. · Macromolecules · 2008 · 41 · 685910.1021/ma801584k ↗
20. Lim R. Y. H. · Science · 2007 · 318 · 64010.1126/science.1145980 ↗
21. Lim R. Y. H. · Proc. Natl. Acad. Sci. U.S.A. · 2006 · 103 · 951210.1073/pnas.0603521103 ↗
22. Schmelmer U. · Small · 2007 · 3 · 45910.1002/smll.200600528 ↗
23. Steenackers M. · Small · 2007 · 3 · 176410.1002/smll.200700187 ↗
24. Adiga S. P. · Nano Lett. · 2002 · 2 · 56710.1021/nl025527j ↗
25. Adiga S. P. · Nano Lett. · 2005 · 5 · 250910.1021/nl051843x ↗
26. Eijkel J. C. T. · Microfluid. Nanofluid. · 2005 · 1 · 24910.1007/s10404-004-0012-9 ↗
27. Al-Amoudi A. · J. Membr. Sci. · 2007 · 303 · 610.1016/j.memsci.2007.06.002 ↗
28. Hong S. K. · J. Membr. Sci. · 1997 · 132 · 15910.1016/S0376-7388(97)00060-4 ↗
29. Zhao B. · Prog. Polym. Sci. · 2000 · 25 · 67710.1016/S0079-6700(00)00012-5 ↗
30. Feldman K. · J. Am. Chem. Soc. · 1999 · 121 · 1013410.1021/ja991049b ↗
31. de Gennes P. G. · Adv. Colloid Interface Sci. · 1987 · 27 · 18910.1016/0001-8686(87)85003-0 ↗
32. de Gennes P. G. · Macromolecules · 1980 · 13 · 106910.1021/ma60077a009 ↗
33. Alexander S. · J. Phys. · 1977 · 38 · 98310.1051/jphys:01977003808098300 ↗
34. O’Shea S. J. · Langmuir · 1993 · 9 · 182610.1021/la00031a034 ↗
35. Butt H. J. · Langmuir · 1999 · 15 · 255910.1021/la981503+ ↗
36. Muller M. T. · Macromolecules · 2005 · 38 · 570610.1021/ma0501545 ↗
37. Koutsos V. · Macromolecules · 1997 · 30 · 471910.1021/ma961625d ↗
38. Halperin A. · Adv. Polym. Sci. · 1992 · 100 · 3110.1007/BFb0051635 ↗
39. Milner S. T. · Science · 1991 · 251 · 90510.1126/science.251.4996.905 ↗
40. Oesterhelt F. · New J. Phys. · 1999 · 1 · 110.1088/1367-2630/1/1/006 ↗
41. Heuberger M. · Biophys. J. · 2005 · 88 · 49510.1529/biophysj.104.045443 ↗
42. Patra M. · Macromolecules · 2006 · 39 · 454010.1021/ma0606410 ↗
43. Koutsioubas A. G. · Langmuir · 2008 · 24 · 1371710.1021/la802536v ↗
44. Asatekin A. · J. Membr. Sci. · 2007 · 298 · 13610.1016/j.memsci.2007.04.011 ↗
45. Denning D. P. · Proc. Natl. Acad. Sci. U.S.A. · 2003 · 100 · 245010.1073/pnas.0437902100 ↗
46. Miao L. L. · Structure · 2009 · 17 · 44910.1016/j.str.2008.12.021 ↗
47. Lim R. Y. H. · Histochem. Cell Biol. · 2008 · 129 · 10510.1007/s00418-007-0371-x ↗
48. Frey S. · Cell · 2007 · 130 · 51210.1016/j.cell.2007.06.024 ↗
49. Patel S. S. · Cell · 2007 · 129 · 8310.1016/j.cell.2007.01.044 ↗
50. Jaggi R. D. · Biophys. J. · 2003 · 84 · 66510.1016/S0006-3495(03)74886-3 ↗
51. Ribbeck K. · EMBO J. · 2002 · 21 · 266410.1093/emboj/21.11.2664 ↗
52. Shulga N. · Mol. Cell. Biol. · 2003 · 23 · 53410.1128/MCB.23.2.534-542.2003 ↗