Biopatterning of Silk Proteins for Soft Micro-optics
Source abstract
Abstract
Silk proteins from spiders and silkworms have been proposed as outstanding candidates for soft micro-optic and photonic applications because of their optical transparency, unique biological properties, and mechanical robustness. Here, we present a method to form microstructures of the two constituent silk proteins, fibroin and sericin for use as an optical biomaterial. Using photolithography, chemically modified silk protein photoresists are patterned in 2D arrays of periodic patterns and Fresnel zone plates. Angle-dependent iridescent colors are produced in these periodic micropatterns because of the Bragg diffraction. Silk protein photolithography can used to form patterns on different substrates including flexible sheets with features of any shape with high fidelity and resolution over large areas. Finally, we show that these mechanically stable and transparent iridescent architectures are also completely biodegradable. This versatile and scalable technique can therefore be used to develop biocompatible, soft micro-optic devices that can be degraded in a controlled manner.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Silk-based biomaterials and applications · Nanofabrication and Lithography Techniques · Biochemical and Structural Characterization
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemical and Life Science Engineering Virginia Commonwealth University, Richmond, Virginia 23284, United States
Department of Biotechnology, Indian Institute of Technology, Kharagpur 721302, India
References (57)
Show source-provided references
1. He Y. · J. Biomed. Nanotechnol. · 2014 · 10 · 76710.1166/jbn.2014.1769 ↗
2. Kim D.-H. · Small · 2012 · 8 · 326310.1002/smll.201200933 ↗
3. Kanellos G. T. · Opt. Express · 2010 · 18 · 17910.1364/OE.18.000179 ↗
4. Lawrence B. D. · Biomacromolecules · 2008 · 9 · 121410.1021/bm701235f ↗
5. Smart S. K. · Carbon · 2006 · 44 · 103410.1016/j.carbon.2005.10.011 ↗
6. Tao H. · Adv. Mater. · 2012 · 24 · 282410.1002/adma.201104477 ↗
7. Azofeifa D. E. · Opt. Mater. · 2012 · 35 · 17510.1016/j.optmat.2012.07.024 ↗
8. Qin G. K. · J. Polym. Sci., Part B:Polym. Phys. · 2013 · 51 · 25410.1002/polb.23204 ↗
9. Domachuk P. · Appl. Phys. Lett. · 2009 · 95 · 253702–110.1063/1.3275719 ↗
10. Der A. · Sens. Actuators, B · 2010 · 151 · 2610.1016/j.snb.2010.09.064 ↗
11. Omenetto F. G. · Nat. Photonics · 2008 · 2 · 64110.1038/nphoton.2008.207 ↗
12. Vepari C. · Prog. Polym. Sci. · 2007 · 32 · 99110.1016/j.progpolymsci.2007.05.013 ↗
13. Aramwit P. · Nat. Prod. Commun. · 2013 · 8 · 501
14. Bhushan B. · Philos. Trans. R. Soc., A · 2009 · 367 · 144510.1098/rsta.2009.0011 ↗
15. Xia Y. · Angew. Chemie., Int. Ed. · 1999 · 37 · 551
16. Tao H. · Proc. Natl. Acad. Sci. U.S.A. · 2012 · 109 · 1958410.1073/pnas.1209056109 ↗
17. Parker S. T. · Adv. Mater. · 2009 · 21 · 241110.1002/adma.200801580 ↗
18. Kim S. · Nat. Photonics · 2012 · 6 · 817
19. Amsden J. J. · Adv. Mater. · 2010 · 22 · 174610.1002/adma.200903166 ↗
20. Gates B. D. · Chem. Rev. · 2005 · 105 · 117110.1021/cr030076o ↗
21. White R. D. · J. Micromech. Microeng · 2011 · 21 · 1110.1088/0960-1317/21/11/115014 ↗
22. Wang J.-N. · Chem.- Asian J. · 2012 · 7 · 30110.1002/asia.201100882 ↗
23. Wu D. · Soft Matter · 2010 · 6 · 26310.1039/B910605G ↗
24. Masuda Y. · Langmuir · 2005 · 21 · 447810.1021/la050075m ↗
25. Sarrat B. · Langmuir · 2011 · 27 · 317410.1021/la104364n ↗
26. Kim S. · Nat. Nanotechnol. · 2014 · 9 · 30610.1038/nnano.2014.47 ↗
27. Galeotti F. · Soft Matter · 2012 · 8 · 481510.1039/c2sm25089f ↗
28. Kurland N. E. · Adv. Mater. · 2013 · 25 · 620710.1002/adma.201302823 ↗
29. Kurland N. E. · Adv. Mater. · 2014 · 26 · 443110.1002/adma.201400777 ↗
30. Nie Z. H. · Nat. Mater. · 2008 · 7 · 27710.1038/nmat2109 ↗
31. Rockwood D. N. · Nat. Protoc. · 2011 · 6 · 161210.1038/nprot.2011.379 ↗
32. Horan R. L. · Biomaterials · 2005 · 26 · 338510.1016/j.biomaterials.2004.09.020 ↗
33. Parker A. R. · Nat. Nanotechnol. · 2007 · 2 · 34710.1038/nnano.2007.152 ↗
34. Vukusic P. · Nature · 2003 · 424 · 85210.1038/nature01941 ↗
35. Glover B. J. · Ann. Bot. · 2010 · 105 · 50510.1093/aob/mcq007 ↗
36. Prum R. O. · Nature · 1998 · 396 · 2810.1038/23838 ↗
37. Seago A. E. · J. R. Soc., Interface · 2009 · 6 · S16510.1098/rsif.2008.0354.focus ↗
38. Bagnara J. T. · Pigm. Cell Res. · 2007 · 20 · 1410.1111/j.1600-0749.2006.00360.x ↗
39. Baez A. V. · J. Opt. Soc. Am. · 1961 · 51 · 40510.1364/JOSA.51.000405 ↗
40. Pang S. · Lab Chip · 2011 · 11 · 369810.1039/c1lc20654k ↗
41. Chien C. C. · Biotechnol. Adv. · 2013 · 31 · 37510.1016/j.biotechadv.2012.04.005 ↗
42. Wu S.-R. · Materials · 2012 · 5 · 175210.3390/ma5101752 ↗
43. Sakdinawat A. · Nat. Photonics · 2010 · 4 · 84010.1038/nphoton.2010.267 ↗
44. Fan Y. H. · Opt. Express · 2003 · 11 · 308010.1364/OE.11.003080 ↗
45. Rajasekharan R. · Adv. Mater. · 2012 · 24 · Op17010.1002/adma.201200296 ↗
46. Morgan B. · J. Microelectromech. Syst. · 2004 · 13 · 11310.1109/JMEMS.2003.823220 ↗
47. Zhao C. X. · Int. J. Biol. Macromol. · 2011 · 48 · 24910.1016/j.ijbiomac.2010.11.004 ↗
48. Arai T. · J. Appl. Polym. Sci. · 2004 · 91 · 238310.1002/app.13393 ↗
49. Zhou C. Z. · Proteins:Struct., Funct., Genet. · 2001 · 44 · 11910.1002/prot.1078 ↗
50. Teramoto H. · Biomacromolecules · 2005 · 6 · 204910.1021/bm0500547 ↗
51. Zuo B. · J. Mater. Sci. · 2006 · 41 · 335710.1007/s10853-005-5384-z ↗
52. Cao Y. · Int. J. Mol. Sci. · 2009 · 10 · 151410.3390/ijms10041514 ↗
53. Hwang S. W. · Science · 2012 · 337 · 164010.1126/science.1226325 ↗
54. Khademhosseini A. · Proc. Natl. Acad. Sci. U.S.A. · 2006 · 103 · 248010.1073/pnas.0507681102 ↗
55. Ainslie K. M. · Lab Chip · 2008 · 8 · 186410.1039/b806446f ↗
56. Altman G. H. · Biomaterials · 2003 · 24 · 40110.1016/S0142-9612(02)00353-8 ↗
57. Panilaitis B. · Biomaterials · 2003 · 24 · 307910.1016/S0142-9612(03)00158-3 ↗