journal article·2015-02-25

Nonfouling Tunable βCD Dextran Polymer Films for Protein Applications

Lars W. Städe, Thorbjørn T. Nielsen, Laurent Duroux, Mogens Hinge, Kyoko Shimizu, Leonid Gurevich, Peter K. Kristensen, Christer Wingren, Kim L. Larsen

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Abstract

Polymeric β-cyclodextrin (βCD) films tunable with respect to thickness and βCD content were prepared in order to develop a suitable platform, allowing for inclusion of nonpolar guest molecules in the βCD cavity, while suppressing nonspecific protein adsorption. The βCD films were synthesized from linear βCD dextran polymers, and grafted onto silicon oxide surfaces by "click" chemistry. Topographic and morphological characteristics are controllable by reaction conditions and polymer type, with average film heights from 2.5 to 12.5 nm. Reversible introduction of electrostatic charges in the βCD dextran by complex formation with 1-adamantanecarboxylic acid prior to surface grafting resulted in a thinner and denser film, presumably by decompaction of the polymers. Total internal reflection fluorescence spectroscopy (TIRF) was employed to evaluate the accessibility of βCD cavities to the fluorescent probe 2-anilinonaphthalene-6-sulfonic acid. Only a minor fraction of the βCD cavities was accessible in the thicker and less dense films; however, accessibility was largely improved with increased ionic strength using NaCl up to 1 M. Antifouling properties of the βCD dextran polymer films were assessed by TIRF real-time monitoring, using bovine serum albumin as a model protein, and showed a 5- to 10-fold reduction in nonspecific adsorption as compared to a bare quartz surface with the degree of reduction reflecting film thickness and interfacial polymer density.
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Research context

OpenAlex topics: Nanofabrication and Lithography Techniques · Innovative Microfluidic and Catalytic Techniques Innovation · Protein purification and stability

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

Affiliations

Department of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Frederik Bajers Vej 7H, DK-9220 Aalborg East, Denmark

Department of Engineering, Aarhus University, Finlandsgade 22, DK-8200 Aarhus, Denmark

Department of Chemistry, Aarhus University, Langelandsgade 140, DK-8000 Aarhus, Denmark

Department of Physics and Nanotechnology, Aalborg University, Skjernvej 4A, DK-9220 Aalborg East, Denmark

Department of Immunotechnology and CREATE Health, Lund University, Medicon Village, SE-22381 Lund, Sweden

Funding

Novo Nordisk · Vetenskapsrådet

References (44)

Show source-provided references
1. Kasemo B. · Surf. Sci. · 2002 · 500 · 65610.1016/S0039-6028(01)01809-X ↗
2. Hildebrand H. · Surf. Coat. Technol. · 2006 · 200 · 631810.1016/j.surfcoat.2005.11.086 ↗
3. Senaratne W. · Biomacromolecules · 2005 · 6 · 242710.1021/bm050180a ↗
4. Rusmini F. · Biomacromolecules · 2007 · 8 · 177510.1021/bm061197b ↗
5. Singh M. · Biotechnol. Adv. · 2002 · 20 · 34110.1016/S0734-9750(02)00020-4 ↗
6. Fragoso A. · Langmuir · 2002 · 18 · 505110.1021/la0256679 ↗
7. Ludden M. J. · Small · 2006 · 2 · 119210.1002/smll.200600147 ↗
8. Jensen R. L. · Langmuir · 2010 · 26 · 1159710.1021/la100950n ↗
9. Yang L. · J. Am. Chem. Soc. · 2012 · 134 · 1919910.1021/ja308450n ↗
10. Uhlenheuer D. A. · Chem.—Eur. J. · 2012 · 18 · 678810.1002/chem.201200238 ↗
11. Duan X. · ACS Nano · 2013 · 7 · 401410.1021/nn306034f ↗
12. Soylemez S. · ACS Appl. Mater. Interfaces · 2014 · 6 · 1829010.1021/am5054493 ↗
13. Leprêtre S. · Biomaterials · 2009 · 30 · 608610.1016/j.biomaterials.2009.07.045 ↗
14. Van de Manakker F. · Biomacromolecules · 2009 · 10 · 315710.1021/bm901065f ↗
15. Shi J. · Nano Lett. · 2010 · 10 · 322310.1021/nl102184c ↗
16. Sobocinski J. · ACS Appl. Mater. Interfaces · 2014 · 6 · 357510.1021/am405774v ↗
17. Ludden M. J. · Angew. Chem. · 2007 · 119 · 418210.1002/ange.200605104 ↗
18. Ludden M. J. · J. Am. Chem. Soc. · 2008 · 130 · 696410.1021/ja078109v ↗
19. González-Campo A. · Small · 2012 · 8 · 353110.1002/smll.201200565 ↗
20. Wasserberg D. · Int. J. Mol. Sci. · 2013 · 14 · 406610.3390/ijms14024066 ↗
21. Petersson L. · Biochim. Biophys. Acta, Proteins Proteomics · 2014 · 1884 · 216410.1016/j.bbapap.2014.08.010 ↗
22. Jonkheijm P. · Angew. Chem., Int. Ed. · 2008 · 47 · 961810.1002/anie.200801711 ↗
23. Onclin S. · Angew. Chem., Int. Ed. · 2005 · 44 · 628210.1002/anie.200500633 ↗
24. Busse S. · Sens. Actuators, B · 2001 · 80 · 11610.1016/S0925-4005(01)00889-9 ↗
25. Onclin S. · Langmuir · 2004 · 20 · 546010.1021/la049561k ↗
26. González-Campo A. · J. Am. Chem. Soc. · 2010 · 132 · 1143410.1021/ja1048658 ↗
27. Piehler J. · Colloids Surf., B · 1999 · 13 · 32510.1016/S0927-7765(99)00046-6 ↗
28. De Sousa Delgado A. · Langmuir · 2001 · 17 · 438610.1021/la001701c ↗
29. Martwiset S. · Langmuir · 2006 · 22 · 819210.1021/la061064b ↗
30. Nielsen T. T. · Biomacromolecules · 2010 · 11 · 171010.1021/bm9013233 ↗
31. Chan T. R. · Org. Lett. · 2004 · 6 · 285310.1021/ol0493094 ↗
32. Das B. · Synthesis · 2007 · 5 · 66610.1055/s-2007-965921 ↗
33. Luzinov I. · Langmuir · 2000 · 16 · 50410.1021/la990500+ ↗
34. Meldal M. · Chem. Rev. · 2008 · 108 · 295210.1021/cr0783479 ↗
35. Rekharsky M. V. · Chem. Rev. · 1998 · 98 · 187510.1021/cr970015o ↗
36. Kawaguchi T. · J. Mater. Sci. Mater. Med. · 2000 · 11 · 3110.1023/A:1008933601813 ↗
37. Frazier R. · Biomaterials · 2000 · 21 · 95710.1016/S0142-9612(99)00270-7 ↗
38. Lummerstorfer T. · J. Phys. Chem. B · 2004 · 108 · 396310.1021/jp049601t ↗
39. Catena G. C. · Anal. Chem. · 1989 · 61 · 90510.1021/ac00183a024 ↗
40. Fülöp Z. · Carbohydr. Polym. · 2013 · 97 · 63510.1016/j.carbpol.2013.05.053 ↗
41. Gonzalez-Gaitano G. · J. Inclusion Phenom. Macrocyclic Chem. · 2002 · 44 · 10110.1023/A:1023065823358 ↗
42. Messner M. · Int. J. Pharm. · 2010 · 387 · 19910.1016/j.ijpharm.2009.11.035 ↗
43. Marcus Y. · Chem. Rev. · 2009 · 109 · 134610.1021/cr8003828 ↗
44. Curry S. · Nat. Struct. Mol. Biol. · 1998 · 5 · 82710.1038/1869 ↗