journal article·2018

Self-standing aptamers by an artificial defect-rich matrix

Chong-You Chen, Chang-Ming Wang, Pai-Shan Chen, Wei-Ssu Liao

Nanoscale· Volume 10· Issue 7
Publisher page

Abstract

The classical alkanethiol post-passivation can prevent nonspecific binding of nucleotide bases onto supporting substrates and help aptamers transition from a "lying down" to a "standing up" orientation. However, the surface probes display lower binding affinity towards targets than those in bulk solutions due to unsatisfied hybridization spaces on the alkanethiol passivated substrate. To overcome this challenge, an artificial defect-rich matrix possessing an aptamer "self-standing" property created by chemical lift-off lithography (CLL) is demonstrated. This approach provided artificial defects on a hydroxyl-terminated alkanethiol self-assembled monolayer (SAM), which allowed the insertion of thiolated aptamers. The diluted surface molecular environment assisted aptamers not only to "self-stand" on the surface, but also to separate from each other, providing a suitable surface aptamer density and sufficient space for capturing targets. With this approach, the binding affinity of the aptamer towards a target was comparable to solution-type probes, showing higher recognition efficiency than that in conventional methods.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Advanced biosensing and bioanalysis techniques · Biosensors and Analytical Detection · Molecular Junctions and Nanostructures

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

Affiliations

Department of Chemistry

National Taiwan University

Taipei 10617

Taiwan

Department and Graduate Institute of Forensic Medicine

Taipei 10002

Funding

Ministry of Science and Technology, Taiwan

References (48)

Show source-provided references
1. Cho · Annu. Rev. Anal. Chem. · 2009 · 2 · 24110.1146/annurev.anchem.1.031207.112851 ↗
2. Liu · Chem. Rev. · 2009 · 109 · 194810.1021/cr030183i ↗
3. Iliuk · Anal. Chem. · 2011 · 83 · 444010.1021/ac201057w ↗
4. Chen · Nanoscale · 2011 · 3 · 54610.1039/C0NR00646G ↗
5. Liu · Nanoscale · 2011 · 3 · 142110.1039/c0nr00887g ↗
6. Herne · J. Am. Chem. Soc. · 1997 · 119 · 891610.1021/ja9719586 ↗
7. Xu · Anal. Chem. · 1993 · 65 · 210210.1021/ac00063a029 ↗
8. Leff · Langmuir · 1996 · 12 · 472310.1021/la960445u ↗
9. Kimura-Suda · J. Am. Chem. Soc. · 2003 · 125 · 901410.1021/ja035756n ↗
10. Levicky · J. Am. Chem. Soc. · 1998 · 120 · 978710.1021/ja981897r ↗
11. Xu · Nanoscale · 2012 · 4 · 378610.1039/c2nr30826f ↗
12. Fang · Nucleic Acids Res. · 1999 · 27 · 194310.1093/nar/27.8.1943 ↗
13. Kick · J. Electron Spectrosc. Relat. Phenom. · 2009 · 172 · 3610.1016/j.elspec.2009.04.002 ↗
14. Aqua · Langmuir · 2003 · 19 · 1057310.1021/la035116y ↗
15. Shuster · Adv. Mater. · 2008 · 20 · 16410.1002/adma.200700082 ↗
16. Murphy · J. Am. Chem. Soc. · 2009 · 131 · 404210.1021/ja808696p ↗
17. Josephs · Nano Lett. · 2012 · 12 · 525510.1021/nl3024356 ↗
18. Goodman · Science · 2005 · 310 · 166110.1126/science.1120367 ↗
19. Bu · Chem. Commun. · 2011 · 47 · 768910.1039/c1cc11628b ↗
20. Mitchell · Angew. Chem., Int. Ed. · 2009 · 48 · 52510.1002/anie.200804264 ↗
21. Lin · Angew. Chem., Int. Ed. · 2015 · 54 · 215110.1002/anie.201410720 ↗
22. Pei · Adv. Mater. · 2010 · 22 · 475410.1002/adma.201002767 ↗
23. Josephs · J. Am. Chem. Soc. · 2012 · 134 · 1002110.1021/ja3010946 ↗
24. Bumm · Science · 1996 · 271 · 170510.1126/science.271.5256.1705 ↗
25. Cygan · J. Am. Chem. Soc. · 1998 · 120 · 272110.1021/ja973448h ↗
26. Shuster · J. Phys. Chem. C · 2011 · 115 · 2477810.1021/jp207396m ↗
27. Claridge · Chem. Soc. Rev. · 2013 · 42 · 272510.1039/C2CS35365B ↗
28. Mullen · Appl. Phys. Lett. · 2007 · 90 · 06311410.1063/1.2457525 ↗
29. Saavedra · Rep. Prog. Phys. · 2010 · 73 · 03650110.1088/0034-4885/73/3/036501 ↗
30. Vaish · ACS Chem. Neurosci. · 2010 · 1 · 49510.1021/cn1000205 ↗
31. Kasemo · Surf. Sci. · 2002 · 500 · 65610.1016/S0039-6028(01)01809-X ↗
32. Tirrell · Surf. Sci. · 2002 · 500 · 6110.1016/S0039-6028(01)01548-5 ↗
33. Smith · Prog. Surf. Sci. · 2004 · 75 · 110.1016/j.progsurf.2003.12.001 ↗
34. Liao · Science · 2012 · 337 · 151710.1126/science.1221774 ↗
35. Liu · Angew. Chem., Int. Ed. · 2006 · 45 · 9010.1002/anie.200502589 ↗
36. Demers · Anal. Chem. · 2000 · 72 · 553510.1021/ac0006627 ↗
37. Andrews · Acc. Chem. Res. · 2016 · 49 · 144910.1021/acs.accounts.6b00034 ↗
38. Cao · ACS Nano · 2015 · 9 · 1143910.1021/acsnano.5b05546 ↗
39. Hermann · Science · 2000 · 287 · 82010.1126/science.287.5454.820 ↗
40. Ligler · Anal. Chem. · 2009 · 81 · 51910.1021/ac8016289 ↗
41. R. R. Chance , A.Prock and R.Silbey , Molecular Fluorescence and Energy Transfer Near Interfaces , in Adv. Chem. Phys , John Wiley & Sons, Inc. , 2007 , pp. 1–65
42. Srinivasan · ACS Nano · 2007 · 1 · 19110.1021/nn7000799 ↗
43. Shuster · Chem. Commun. · 2011 · 47 · 1064110.1039/c1cc13002a ↗
44. Stojanovic · J. Am. Chem. Soc. · 2001 · 123 · 492810.1021/ja0038171 ↗
45. Neves · Biochemistry · 2010 · 49 · 847810.1021/bi100952k ↗
46. Neves · Biophys. Chem. · 2010 · 153 · 910.1016/j.bpc.2010.09.009 ↗
47. White · Langmuir · 2008 · 24 · 1051310.1021/la800801v ↗
48. Baker · J. Am. Chem. Soc. · 2006 · 128 · 313810.1021/ja056957p ↗