Preparation and mechanical properties of layers made of recombinant spider silk proteins and silk from silk worm
Source abstract
Abstract
Layers of recombinant spider silks and native silks from silk worms were prepared by spin-coating and casting of various solutions. FT-IR spectra were recorded to investigate the influence of the different mechanical stress occurring during the preparation of the silk layers. The solubility of the recombinant spider silk proteins SO1-ELP, C16, AQ24NR3, and of the silk fibroin from Bombyx mori were investigated in hexafluorisopropanol, ionic liquids and concentrated salt solutions. The morphology and thickness of the layers were determined by Atomic Force Microscopy (AFM) or with a profilometer. The mechanical behaviour was investigated by acoustic impedance analysis by using a quartz crystal microbalance (QCMB) as well as by microindentation. The density of silk layers (d<300 nm) was determined based on AFM and QCMB measurements. At silk layers thicker than 300 nm significant changes of the half-band-half width can be correlated with increasing energy dissipation. Microhardness measurements demonstrate that recombinant spider silk and sericine-free Bombyx mori silk layers achieve higher elastic penetration modules EEP and Martens hardness values HM than those of polyethylenterephthalate (PET) and polyetherimide (PEI) foils.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Silk-based biomaterials and applications · Silkworms and Sericulture Research · Invertebrate Immune Response Mechanisms
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (30)
Show source-provided references
1. Rising A, Nimmervoll H, Grip S, Fernandez-Arias A, Storckenfeldt E, Knight DP, Vollrath F, Engström W (2005) Zool. Sci. 22:27310.2108/zsj.22.273 ↗
2. Pérez-Rigueiro J, Elices M, Guinea GV (2003) Polymer 44:373310.1016/S0032-3861(03)00245-3 ↗
3. Vollrath F (2000) Mol. Biotechn. 74:6710.1016/S1389-0352(00)00006-4 ↗
4. Shao Z, Vollrath F (2002) Nature 418:74110.1038/418741a ↗
5. Altman GH, Diaz F, Jakuba C, Calabro T, Horan RL, Chen J, Lu H, Richmond J, Kaplan DL (2003) Biomaterials 24:40110.1016/S0142-9612(02)00353-8 ↗
6. Minoura N, Aiba S, Gotoh Y, Tsukada M, Imai Y (1995) J. Biomed. Mater. Res. 29:121510.1002/jbm.820291008 ↗
7. Sofia S, McCarthy MB, Gronowicz G, Kaplan DL (2001) J. Biomed. Mater. Res. 54:13910.1002/1097-4636(200101)54:1<139::AID-JBM17>3.0.CO;2-7 ↗
8. Altman GH, Horan RL, Lu HH, Moreau J, Martin I, Richmond JC, Kaplan DL (2002) Biomaterials 23:413110.1016/S0142-9612(02)00156-4 ↗
9. Meinel L, Hoffmann S, Karageorgiou V, Zichner L, Langer R, Kaplan DL (2004) Biotechnol. Bioeng. 88:37910.1002/bit.20252 ↗
10. Meinel L, Karageorgiou V, Hoffmann S, Fajardo R, Snyder B, Li L, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL (2004) J. Biomed. Mater. Res. 71A:2510.1002/jbm.a.30117 ↗
11. Karageorgiou V, Meinel L, Hoffmann S, Malhotra A, Voloch V, Kaplan DL (2004) J. Biomed. Mater. Res. 71A:52810.1002/jbm.a.30186 ↗
12. J. Rosenbloom, W.R. Abrams, R. Mecham, Faseb J, 7:1208 (1993)10.1096/fasebj.7.13.8405806 ↗
13. Scheller J, Henggeler D, Viviani A, Conrad U (2004) Transgenic Res. 13:5110.1023/B:TRAG.0000017175.78809.7a ↗
14. Muller WS, Samuelson LA, Fossey SA, Kaplan DL (1993) Langmuir 9:185710.1021/la00031a038 ↗
15. Putthanarat S, Zarkoop S, Magoshi J, Chen JA, Eby RK, Stone M, Adams WW (2002) Polymer 43:340510.1016/S0032-3861(02)00161-1 ↗
16. Zhao C, Yao J, Masuda H, Kishore R, Asakura T (2003) Biopolymers 69:25310.1002/bip.10350 ↗
17. Arai T, Freddi G, Innocenti R, Tsukada M (2004) J. Appl. Polym. Sci. 91:238310.1002/app.13393 ↗
18. Motta A, Fambri L, Migliaresi C (2002) Macromol. Chem. Phys. 203:1658
19. Scheller J, Gührs K-H, Grosse F, Conrad U (2001) Nature Biotechnol. 19:573
20. J. Scheller, U. Conrad, Molecular Farming. Edited by R. Fischer, S. Schillberg (Wiley-VCH 2004) p. 17110.1002/3527603638.ch11 ↗
21. Huemmerich D, Helsen CW, Quedzuweit S, Oschmann J, Rudolph R, Scheibel T (2004) Biochemistry 43:1360410.1021/bi048983q ↗
22. T. Scheibel, personal communication (2005)
23. Meyer E, Chilkoti A (1999) Nature Biotechnol. 17:1112
24. Zhou C-Z, Confalonieri F, Jacquet M, Rerasso RP, Li Z-G, Janin J (2001) Proteins 44:11910.1002/prot.1078 ↗
25. Johannsmann D (1999) Macromol. Chem. Phys. 200:501
26. T. Chudoba, Haerte 4.5, Asmec GmbH, Radeberg, Germany (www.asmec.de)
27. Phillips M, Drummy LF, Conrady DG, Fox DM, Naik RR, Stone MO, Trulove PC, De Long HC, Mantz RA (2004) J. Am. Chem. Soc. 126:1435010.1021/ja046079f ↗
28. Smith PK, Krohn RI, Hermanson GT, Malla AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC (1985) Anal. Biochem. 150:7610.1016/0003-2697(85)90442-7 ↗
29. G. Sauerbrey, Arch. Elektrotech. Übertragung 18:617 (1964)
30. Puente Orench I, Putthanarat S, Balta Calleja FJ, Ebby RK, Stone M (2004) Polymer 45:204110.1016/j.polymer.2003.12.069 ↗