journal article·2017-04-05

Clickable Antifouling Polymer Brushes for Polymer Pen Lithography

Uwe Bog, Andres de los Santos Pereira, Summer L. Mueller, Shana Havenridge, Viviana Parrillo, Michael Bruns, Andrea E. Holmes, Cesar Rodriguez-Emmenegger, Harald Fuchs, Michael Hirtz

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Abstract

Protein-repellent reactive surfaces that promote localized specific binding are highly desirable for applications in the biomedical field. Nonspecific adhesion will compromise the function of bioactive surfaces, leading to ambiguous results of binding assays and negating the binding specificity of patterned cell-adhesive motives. Localized specific binding is often achieved by attaching a linker to the surface, and the other side of the linker is used to bind specifically to a desired functional agent, as e.g. proteins, antibodies, and fluorophores, depending on the function required by the application. We present a protein-repellent polymer brush enabling highly specific covalent surface immobilization of biorecognition elements by strain-promoted alkyne-azide cycloaddition click chemistry for selective protein adhesion. The protein-repellent polymer brush is functionalized by highly localized molecular binding sites in the low micrometer range using polymer pen lithography (PPL). Because of the massive parallelization of writing pens, the tunable PPL printed patterns can span over square centimeter areas. The selective binding of the protein streptavidin to these surface sites is demonstrated while the remaining polymer brush surface is resisting nonspecific adsorption without any prior blocking by bovine serum albumin (BSA). In contrast to the widely used BSA blocking, the reactive polymer brushes are able to significantly reduce nonspecific protein adsorption, which is the cause of biofouling. This was achieved for solutions of single proteins as well as complex biological fluids. The remarkable fouling resistance of the polymer brushes has the potential to improve the multiplexing capabilities of protein probes and therefore impact biomedical research and applications.
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Research context

OpenAlex topics: Nanofabrication and Lithography Techniques · Polymer Surface Interaction Studies · Force Microscopy Techniques and Applications

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

Affiliations

Department of Chemistry and Physics of Surfaces and Biointerfaces, Institute of Macromolecular Chemistry ASCR, v.v.i., Prague, Czech Republic

Department of Chemistry, Doane University, Crete, Nebraska, and the Center for Nanohybrid Functional Materials (CNFM), University of Nebraska—Lincoln, Lincoln, Nebraska 68588, United States

DWI − Leibniz Institute for Interactive Materials and Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, Aachen, Germany

Physical Institute & Center for Nanotechnology (CeNTech), University of Münster, Münster, Germany

Funding

European Regional Development Fund · Grantov? Agentura Cesk? Republiky · National Science Foundation · Center for Chemical Polymer Technology · North Rhine-Westphalia

References (52)

Show source-provided references
1. 10.1021/acsbiomaterials.5b0040310.1021/acsbiomaterials.5b00403 ↗
2. 10.1039/C5MH00089K10.1039/C5MH00089K ↗
3. 10.1021/acsami.5b0945910.1021/acsami.5b09459 ↗
4. 10.3390/ijms1208513510.3390/ijms12085135 ↗
5. 10.1016/j.vascn.2009.12.00210.1016/j.vascn.2009.12.002 ↗
6. 10.1155/2012/70786310.1155/2012/707863 ↗
7. 10.1016/j.bios.2013.07.01510.1016/j.bios.2013.07.015 ↗
8. 10.1021/la204777x10.1021/la204777x ↗
9. 10.1016/j.biomaterials.2005.11.02710.1016/j.biomaterials.2005.11.027 ↗
10. 10.1021/la026178b10.1021/la026178b ↗
11. 10.1039/c3lc50149c10.1039/c3lc50149c ↗
12. 10.1002/smll.20140081310.1002/smll.201400813 ↗
13. 10.1002/advs.20150006610.1002/advs.201500066 ↗
14. 10.1016/j.biomaterials.2009.10.01710.1016/j.biomaterials.2009.10.017 ↗
15. Thompson M. · 201610.1039/9781782622048 ↗
16. 10.1039/C4PY00281D10.1039/C4PY00281D ↗
17. 10.1007/s00216-015-8606-510.1007/s00216-015-8606-5 ↗
18. 10.1039/C5BM00085H10.1039/C5BM00085H ↗
19. 10.1002/adma.20130249210.1002/adma.201302492 ↗
20. 10.1016/j.bios.2013.12.01110.1016/j.bios.2013.12.011 ↗
21. 10.1021/nl504183610.1021/nl5041836 ↗
22. 10.1016/j.snb.2014.06.07510.1016/j.snb.2014.06.075 ↗
23. 10.1021/acs.langmuir.5b0111410.1021/acs.langmuir.5b01114 ↗
24. 10.1126/science.116219310.1126/science.1162193 ↗
25. 10.1126/science.283.5402.66110.1126/science.283.5402.661 ↗
26. 10.1002/smll.20137011910.1002/smll.201370119 ↗
27. 10.1002/smll.20090153810.1002/smll.200901538 ↗
28. 10.1002/smll.20110270710.1002/smll.201102707 ↗
29. 10.1002/smll.20160162310.1002/smll.201601623 ↗
30. 10.1021/ja404207710.1021/ja4042077 ↗
31. 10.1002/1521-3773(20010601)40:11<2004::AID-ANIE2004>3.0.CO;2-510.1002/1521-3773(20010601)40:11<2004::AID-ANIE2004>3.0.CO;2-5 ↗
32. 10.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-410.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-4 ↗
33. 10.1021/ol061094610.1021/ol0610946 ↗
34. 10.1021/ja021381e10.1021/ja021381e ↗
35. 10.1002/anie.20090094210.1002/anie.200900942 ↗
36. 10.1039/C6RA12194B10.1039/C6RA12194B ↗
37. 10.1021/la011365f10.1021/la011365f ↗
38. 10.1038/nprot.2013.15910.1038/nprot.2013.159 ↗
39. 10.1016/0368-2048(76)80015-110.1016/0368-2048(76)80015-1 ↗
40. 10.1002/sia.74021030210.1002/sia.740210302 ↗
41. 10.1016/S1359-0286(97)80125-810.1016/S1359-0286(97)80125-8 ↗
42. 10.1039/c3py00103b10.1039/c3py00103b ↗
43. 10.1021/la052947q10.1021/la052947q ↗
44. 10.1021/jp409338y10.1021/jp409338y ↗
45. 10.1021/ja905409610.1021/ja9054096 ↗
46. 10.1073/pnas.091111610710.1073/pnas.0911116107 ↗
47. 10.1515/nanofab-2015-000510.1515/nanofab-2015-0005 ↗
48. 10.1002/anie.20090264910.1002/anie.200902649 ↗
49. 10.1016/S0065-3233(08)60411-810.1016/S0065-3233(08)60411-8 ↗
50. 10.1002/mabi.20120017110.1002/mabi.201200171 ↗
51. 10.1021/la900083s10.1021/la900083s ↗
52. 10.1039/9781849737302-0000110.1039/9781849737302-00001 ↗