journal article·2019Open access

Single molecule protein patterning using hole mask colloidal lithography

William Lum, Dinesh Gautam, Jixin Chen, Laura B. Sagle

Nanoscale· Volume 11· Issue 35

Abstract

The ability to manipulate single protein molecules on a surface is useful for interfacing biology with many types of devices in optics, catalysis, bioengineering, and biosensing. Control of distance, orientation, and activity at the single molecule level will allow for the production of on-chip devices with increased biological activity. Cost effective methodologies for single molecule protein patterning with tunable pattern density and scalable coverage area remain a challenge. Herein, Hole Mask Colloidal Lithography is presented as a bench-top colloidal lithography technique that enables a glass coverslip to be patterned with functional streptavidin protein onto patches from 15-200 nm in diameter with variable pitch. Atomic force microscopy (AFM) was used to characterize the size of the patterned features on the glass surface. Additionally, single-molecule fluorescence microscopy was used to demonstrate the tunable pattern density, measure binding controls, and confirm patterned single molecules of functional streptavidin.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Nanofabrication and Lithography Techniques · Monoclonal and Polyclonal Antibodies Research · Advanced Biosensing Techniques and Applications

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

Affiliations

Department of Chemistry

College of Arts and Sciences

University of Cincinnati

Cincinnati OH 45221-0172

USA

Department of Chemistry and Biochemistry

Ohio University

Athens

Funding

National Institutes of Health

References (47)

Show source-provided references
1. Mrksich · Trends Biotechnol. · 1995 · 13 · 22810.1016/S0167-7799(00)88950-7 ↗
2. Howell · Langmuir · 2003 · 19 · 43610.1021/la026365+ ↗
3. Cho · Anal. Chem. · 2002 · 74 · 617710.1021/ac020454+ ↗
4. Asphahani · Analyst · 2007 · 132 · 83510.1039/b704513a ↗
5. Yu · Theranostics · 2017 · 7 · 405710.7150/thno.20151 ↗
6. You · Expert Opin. Drug Discovery · 2016 · 11 · 10510.1517/17460441.2016.1109625 ↗
7. Mateo · Enzyme Microb. Technol. · 2007 · 40 · 145110.1016/j.enzmictec.2007.01.018 ↗
8. Wang · Catalysts · 2018 · 8 · 16610.3390/catal8040166 ↗
9. Hou · Angew. Chem., Int. Ed. · 2018 · 57 · 254410.1002/anie.201704752 ↗
10. Campagnola · Nat. Biotechnol. · 2003 · 21 · 135610.1038/nbt894 ↗
11. Qiuming · Langmuir · 2007 · 23 · 865910.1021/la7007073 ↗
12. Neumann · ChemBioChem · 2002 · 3 · 99310.1002/1439-7633(20021004)3:10<993::AID-CBIC993>3.0.CO;2-Y ↗
13. Hengsakul · Bioconjugate Chem. · 1996 · 7 · 24910.1021/bc960007z ↗
14. Welch · Biointerphases · 2017 · 12 · 02D30110.1116/1.4978435 ↗
15. Olmsted · Anal. Chem. · 2012 · 84 · 1081710.1021/ac302933h ↗
16. B. Douzi , in Methods in Molecular Biology , Humana Press , New York, NY , 2017 , vol. 1615 , pp. 257–275
17. Uetz · Nature · 2000 · 403 · 62310.1038/35001009 ↗
18. Koeller · Nature · 2001 · 409 · 23210.1038/35051706 ↗
19. Chen · Prog. Mater. Sci. · 2012 · 57 · 149210.1016/j.pmatsci.2012.03.001 ↗
20. Barber · Chem. Soc. Rev. · 2009 · 38 · 18510.1039/B802262N ↗
21. Koirala · Angew. Chem., Int. Ed. · 2014 · 53 · 813710.1002/anie.201404043 ↗
22. Ngo · Anal. Bioanal. Chem. · 2014 · 406 · 333510.1007/s00216-014-7648-4 ↗
23. Palma · J. Am. Chem. Soc. · 2011 · 133 · 765610.1021/ja201031g ↗
24. Lau · ACS Nano · 2016 · 10 · 72310.1021/acsnano.5b05781 ↗
25. Schvartzman · Nano Lett. · 2011 · 11 · 130610.1021/nl104378f ↗
26. Michalet · Chem. Rev. · 2006 · 106 · 178510.1021/cr0404343 ↗
27. Kawai · Proc. Natl. Acad. Sci. U. S. A. · 2014 · 111 · 396810.1073/pnas.1319938111 ↗
28. Ariga · Chem. Soc. Rev. · 2013 · 42 · 632210.1039/c2cs35475f ↗
29. Renault · J. Phys. Chem. B · 2003 · 107 · 70310.1021/jp0263424 ↗
30. Romanov · Analyst · 2014 · 139 · 130310.1039/C3AN01577G ↗
31. Kenseth · Langmuir · 2001 · 17 · 410510.1021/la0100744 ↗
32. Zhang · Small · 2005 · 1 · 83310.1002/smll.200500091 ↗
33. Ramakrishnan · ACS Appl. Mater. Interfaces · 2016 · 8 · 3123910.1021/acsami.6b10535 ↗
34. Killops · ACS Macro Lett. · 2012 · 1 · 75810.1021/mz300153k ↗
35. Kolodziej · Chem. Mater. · 2012 · 24 · 77410.1021/cm202669f ↗
36. Zhang · Small · 2005 · 1 · 83310.1002/smll.200500091 ↗
37. Min · Adv. Mater. · 2008 · 20 · 355010.1002/adma.200800569 ↗
38. Kumar · Langmuir · 2005 · 21 · 665210.1021/la050331v ↗
39. Lee · ACS Nano · 2018 · 12 · 164210.1021/acsnano.7b08226 ↗
40. Fredriksson · Adv. Mater. · 2007 · 19 · 429710.1002/adma.200700680 ↗
41. Jokinen · Biomicrofluidics · 2012 · 6 · 1650110.1063/1.3673251 ↗
42. Chen · J. Biomed. Mater. Res., Part A · 2018 · 106 · 186210.1002/jbm.a.36383 ↗
43. Navarre · Langmuir · 2001 · 17 · 484410.1021/la001358b ↗
44. Giamblanco · ACS Omega · 2017 · 2 · 130910.1021/acsomega.7b00007 ↗
45. Liu · Environ. Sci. Technol. · 2018 · 52 · 272610.1021/acs.est.7b05622 ↗
46. Vashist · Diagnostics · 2012 · 2 · 2310.3390/diagnostics2030023 ↗
47. Caswell · J. Am. Chem. Soc. · 2003 · 125 · 1391410.1021/ja037969i ↗