Modulating Materials by Orthogonally Oriented β‐Strands: Composites of Amyloid and Silk Fibroin Fibrils
Source abstract
Abstract
Amyloid fibrils and silk fibroin (SF) fibrils are proteinaceous aggregates occurring either naturally or as artificially reconstituted fibrous systems, in which the constituent β-strands are aligned either orthogonally or parallel to the fibril main axis, conferring complementary physical properties. Here, it is shown how the combination of these two classes of protein fibrils with orthogonally oriented β-strands results in composite materials with controllable physical properties at the molecular, mesoscopic, and continuum length scales. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Silk-based biomaterials and applications · Polydiacetylene-based materials and applications · Bone Tissue Engineering Materials
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Food & Soft Materials Science Institute of Food Nutrition & Health ETH Zürich LFO23 Schmelzbergstrasse 9 8092 Zürich Switzerland
State Key Laboratory of Molecular Engineering of Polymers Department of Macromolecular Science Laboratory of Advanced Materials Fudan University Shanghai 200433 PR China
References (38)
Show source-provided references
1. 10.1038/3506900010.1038/35069000 ↗
2. 10.1038/nnano.2011.10210.1038/nnano.2011.102 ↗
3. 10.1002/anie.20070313310.1002/anie.200703133 ↗
4. 10.1021/ma202157h10.1021/ma202157h ↗
5. 10.3402/nano.v2i0.603210.3402/nano.v2i0.6032 ↗
6. 10.1038/418741a10.1038/418741a ↗
7. 10.1046/j.1432-1033.2002.03112.x10.1046/j.1432-1033.2002.03112.x ↗
8. 10.1021/nl101341w10.1021/nl101341w ↗
9. 10.1038/nature1073910.1038/nature10739 ↗
10. 10.1016/S0945-053X(98)90023-310.1016/S0945-053X(98)90023-3 ↗
11. 10.1016/j.jsb.2009.03.00110.1016/j.jsb.2009.03.001 ↗
12. 10.1679/aohc.65.10910.1679/aohc.65.109 ↗
13. 10.1016/S1369-7021(12)70091-310.1016/S1369-7021(12)70091-3 ↗
14. 10.1016/j.pmatsci.2008.06.00210.1016/j.pmatsci.2008.06.002 ↗
15. 10.1016/S0962-8924(00)01828-610.1016/S0962-8924(00)01828-6 ↗
16. 10.1039/c3cp00067b10.1039/c3cp00067b ↗
17. 10.1039/b919453n10.1039/b919453n ↗
18. 10.1002/mabi.20060020110.1002/mabi.200600201 ↗
19. 10.1038/nnano.2010.5910.1038/nnano.2010.59 ↗
20. 10.1039/c2nr30768e10.1039/c2nr30768e ↗
21. 10.1002/adma.20080133210.1002/adma.200801332 ↗
22. 10.1039/b911049f10.1039/b911049f ↗
23. 10.1021/mz400639y10.1021/mz400639y ↗
24. 10.1038/nnano.2012.6210.1038/nnano.2012.62 ↗
25. 10.1038/nnano.2010.2610.1038/nnano.2010.26 ↗
26. 10.1002/adma.20130142910.1002/adma.201301429 ↗
27. 10.1016/j.progpolymsci.2011.07.00310.1016/j.progpolymsci.2011.07.003 ↗
28. 10.1002/adma.20080058210.1002/adma.200800582 ↗
29. 10.1038/nprot.2011.37910.1038/nprot.2011.379 ↗
30. 10.1039/b914218e10.1039/b914218e ↗
31. 10.1039/b913510c10.1039/b913510c ↗
32. 10.1021/la101636r10.1021/la101636r ↗
33. 10.1021/la902143210.1021/la9021432 ↗
34. 10.1007/s00339-005-3425-810.1007/s00339-005-3425-8 ↗
35. 10.1016/j.actbio.2009.10.04110.1016/j.actbio.2009.10.041 ↗
36. 10.1073/pnas.15216229910.1073/pnas.152162299 ↗
37. 10.1016/S0142-9612(02)00353-810.1016/S0142-9612(02)00353-8 ↗
38. 10.1016/j.biomaterials.2008.11.01810.1016/j.biomaterials.2008.11.018 ↗