journal article·2015-06-17

Directed Growth of Virus Nanofilaments on a Superhydrophobic Surface

Giovanni Marinaro, Manfred Burghammer, Luca Costa, Thomas Dane, Francesco De Angelis, Enzo Di Fabrizio, Christian Riekel

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Abstract

The evaporation of single droplets of colloidal tobacco mosaic virus (TMV) nanoparticles on a superhydrophobic surface with a hexagonal pillar-pattern results in the formation of coffee-ring type residues. We imaged surface features by optical, scanning electron, and atomic force microscopies. Bulk features were probed by raster-scan X-ray nanodiffraction. At ∼100 pg/μL nanoparticle concentration, the rim of the residue connects to neighboring pillars via fibrous extensions containing flow-aligned crystalline domains. At ∼1 pg/μL nanoparticle concentration, nanofilaments of ≥80 nm diameter and ∼20 μm length are formed, extending normal to the residue-rim across a range of pillars. X-ray scattering is dominated by the nanofilament form-factor but some evidence for crystallinity has been obtained. The observation of sheets composed of stacks of self-assembled nanoparticles deposited on pillars suggests that the nanofilaments are drawn from a structured droplet interface.
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Research context

OpenAlex topics: Nanomaterials and Printing Technologies · Plasmonic and Surface Plasmon Research · Fluid Dynamics and Thin Films

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

Affiliations

ESRF-European Synchrotron Radiation Facility, CS 40220, F-38043 Grenoble Cedex 9, France

Nanostructures Department, Istituto Italiano di Tecnologia, Via Morego 30, Genova 16163, Italy

Department of Analytical Chemistry, Ghent University, Krijgslaan 281, S12B-9000 Ghent, Belgium

Physical Science and Engineering Divisions, KAUST (King Abdullah University of Science and Technology) , Jeddah, Saudi Arabia

BIONEM Lab, University of Magna Graecia, Campus Salvatore Venuta, Viale Europa, 88100 Germaneto-Catanzaro, Italy

References (47)

Show source-provided references
1. Ryan A. J. · 1999 · 739
2. Zafeiropoulos N. · Macromol. Rapid Commun. · 2005 · 26 · 154710.1002/marc.200500428 ↗
3. Martel A. · Biomicrofluidics · 2008 · 2 · 02410410.1063/1.2943732 ↗
4. Martel A. · J. Am. Chem. Soc. · 2008 · 130 · 1707010.1021/ja806654t ↗
5. Berthier J. · 2008
6. Accardo A. · J. Synchrotron Radiat. · 2014 · 21 · 64310.1107/S1600577514009849 ↗
7. Deegan R. D. · Nature · 1997 · 389 · 82710.1038/39827 ↗
8. Gentile F. · Nano Lett. · 2012 · 12 · 645310.1021/nl3039162 ↗
9. Henegariu O. · Biotechniques · 2001 · 31 · 24610.2144/01312bm01 ↗
10. Kendall A. · J. Virol. · 2008 · 82 · 954610.1128/JVI.00895-08 ↗
11. Gebhardt R. · Soft Matter · 2014 · 10 · 545810.1039/C4SM00414K ↗
12. Caspar D. L. D. · Adv. Protein Chem. · 1963 · 18 · 3710.1016/S0065-3233(08)60268-5 ↗
13. Klug A. · Philos. Trans. R. Soc., B · 1999 · 354 · 53110.1098/rstb.1999.0404 ↗
14. Dogic Z. · Curr. Opin. Colloid Interface Sci. · 2006 · 11 · 4710.1016/j.cocis.2005.10.004 ↗
15. Lu B. · Virology · 1996 · 225 · 1110.1006/viro.1996.0570 ↗
16. Yang L. · Soft Matter · 2009 · 5 · 495110.1039/b911894b ↗
17. Britt D. W. · Thin Solid Films · 1998 · 327 · 82410.1016/S0040-6090(98)00770-6 ↗
18. Wargacki S. P. · Langmuir · 2008 · 24 · 543910.1021/la7040778 ↗
19. Dogic Z. · J. Chem. Phys. · 2000 · 113 · 836810.1063/1.1308107 ↗
20. Rammensee S. · Proc. Natl. Acad. Sci. U. S. A. · 2008 · 105 · 659010.1073/pnas.0709246105 ↗
21. Heddle J. G. · Nanotechnol., Sci. Appl. · 2008 · 1 · 6710.2147/NSA.S4092 ↗
22. Rong J. H. · J. Mater. Chem. · 2009 · 19 · 284110.1039/b901130g ↗
23. Uchida M. · Adv. Mater. · 2007 · 19 · 102510.1002/adma.200601168 ↗
24. Schlick T. L. · J. Am. Chem. Soc. · 2005 · 127 · 371810.1021/ja046239n ↗
25. Kuncicky D. M. · Small · 2006 · 2 · 146210.1002/smll.200600399 ↗
26. Knez M. · Adv. Funct. Mater. · 2004 · 14 · 11610.1002/adfm.200304376 ↗
27. Niu Z. · Chem. Commun. · 2006 · 301910.1039/b603780a ↗
28. Niu Z. · Langmuir · 2007 · 23 · 671910.1021/la070096b ↗
29. Niu Z. · Nano Lett. · 2007 · 7 · 372910.1021/nl072134h ↗
30. Gerasopoulos K. · ACS Nano · 2012 · 6 · 642210.1021/nn301981p ↗
31. Miele E. · Adv. Mater. · 2014 · 26 · 417910.1002/adma.201400310 ↗
32. Limongi T. · Small · 2013 · 9 · 40210.1002/smll.201201377 ↗
33. Marinaro G. · Lab Chip · 2014 · 14 · 370510.1039/C4LC00750F ↗
34. Mueller M. · Macromolecules · 1998 · 31 · 395310.1021/ma980004c ↗
35. Schroer C. G. · Phys. Rev. Lett. · 2008 · 101 · 09080110.1103/PhysRevLett.101.090801 ↗
36. Riekel C. · 2008
37. Stark M. · Biophys. J. · 2001 · 80 · 300910.1016/S0006-3495(01)76266-2 ↗
38. Oliver J. F. · J. Colloid Interface Sci. · 1977 · 59 · 56810.1016/0021-9797(77)90052-2 ↗
39. Accardo A. · Lab Chip · 2013 · 13 · 33210.1039/C2LC41193H ↗
40. Glatter O. · 1982
41. Ziabicki A. · 1976
42. Vollrath F. · Nature · 2001 · 410 · 54110.1038/35069000 ↗
43. Vendrely C. · Methods Mol. Biol. · 2008 · 474 · 310.1007/978-1-59745-480-3_1 ↗
44. Stark M. · Biomacromolecules · 2007 · 8 · 169510.1021/bm070049y ↗
45. Oroudjev E. · Proc. Natl. Acad. Sci. U.S.A. · 2002 · 99 · 646010.1073/pnas.082526499 ↗
46. Ling S. · ACS Macro Lett. · 2014 · 3 · 14610.1021/mz400639y ↗
47. Knowles T. P. J. · Nat. Nanotechnol. · 2011 · 6 · 46910.1038/nnano.2011.102 ↗