Fluorination Induced Inversion of Helicity and Self‐Assembly Into Cross‐α Like Piezoelectric Amyloids by Minimalistic Designer Peptide
Source abstract
Abstract
Abstract Although initially identified as pathological aggregates, amyloid fibrillar assemblies formed by various proteins and peptides are now known to have crucial physiological roles, carrying out numerous biological functions in almost all organisms. Due to unique features, the common etiology of amyloids’ cross‐β structure is long posited as a template for designing artificial self‐assembling systems. However, the recent discovery of cross‐α amyloids indicates additional structural paradigms for self‐assembly into ordered nanostructures, turning significant attention toward designing artificial nanostructures based on cross‐α assembly. Herein, a minimalistic designer peptide which forms a hydrogen‐bonded amyloid‐like structure while remaining in the α region of conformation is engineered, to investigate the effect of aromatic, hydrophobic, and steric considerations on amyloidal assemblies. These results demonstrate a significant modulation of helicity and self‐assembly, leading to the structure‐dependent piezoelectric function of the amyloid‐like cross‐α fibrils. This study indicates a potential avenue for molecular engineering of functional peptide materials.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Polydiacetylene-based materials and applications · Luminescence and Fluorescent Materials
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemistry Ashoka University Sonipat Haryana 131029 India
Department of Biochemistry & Chemistry La Trobe Institute for Molecular Science (LIMS) La Trobe University Melbourne Victoria 3086 Australia
Key Laboratory of Biorheological Science and Technology Ministry of Education College of Bioengineering Chongqing University Chongqing 400044 China
Department of Physics and Materials Science University of Luxembourg Luxembourg City L‐1511 Luxembourg
Department of Chemical Research Support Weizmann Institute of Science Rehovot 76100 Israel
Department of Chemical Sciences Bernal Institute University of Limerick Limerick V94 T9PX Ireland
SSPC The Science Foundation Ireland Research Centre for Pharmaceuticals University of Limerick Limerick V94 T9PX Ireland
The Biomedical and Environmental Sensor Technology (BEST) Research Centre Biosensors Program La Trobe Institute for Molecular Science (LIMS) La Trobe University Melbourne Victoria 3086 Australia
Funding
National Natural Science Foundation of China · HORIZON EUROPE European Research Council · Science Foundation Ireland
References (100+)
Show source-provided references
1. 10.1038/s41580-018-0060-810.1038/s41580-018-0060-8 ↗
2. 10.1039/C9CS00199A10.1039/C9CS00199A ↗
3. 10.1016/j.cell.2021.08.01310.1016/j.cell.2021.08.013 ↗
4. 10.1039/D2CS00756H10.1039/D2CS00756H ↗
5. 10.1039/C6CS00542J10.1039/C6CS00542J ↗
6. 10.1126/science.aaf490110.1126/science.aaf4901 ↗
7. 10.1021/ar050071910.1021/ar0500719 ↗
8. 10.1038/s41589-018-0105-510.1038/s41589-018-0105-5 ↗
9. 10.1038/s41467-020-20689-w10.1038/s41467-020-20689-w ↗
10. 10.1038/s41563-019-0343-210.1038/s41563-019-0343-2 ↗
11. 10.1016/j.tibs.2024.10.00410.1016/j.tibs.2024.10.004 ↗
12. 10.1039/C1CS15241F10.1039/C1CS15241F ↗
13. 10.1021/acs.accounts.7b0022610.1021/acs.accounts.7b00226 ↗
14. 10.1073/pnas.112011210910.1073/pnas.1120112109 ↗
15. 10.1002/prot.2217710.1002/prot.22177 ↗
16. 10.1021/bi002258810.1021/bi0022588 ↗
17. 10.1002/cbic.20070064310.1002/cbic.200700643 ↗
18. 10.1021/ja004351p10.1021/ja004351p ↗
19. 10.1002/prot.112310.1002/prot.1123 ↗
20. 10.1016/j.bmcl.2009.07.09310.1016/j.bmcl.2009.07.093 ↗
21. 10.1021/ja063457310.1021/ja0634573 ↗
22. 10.1002/anie.20100286010.1002/anie.201002860 ↗
23. 10.1073/pnas.080029110510.1073/pnas.0800291105 ↗
24. 10.1021/ja026668q10.1021/ja026668q ↗
25. 10.1021/bi400027y10.1021/bi400027y ↗
26. 10.1021/ja301328f10.1021/ja301328f ↗
27. 10.1039/C0MB00210K10.1039/C0MB00210K ↗
28. 10.1039/C3SC52932K10.1039/C3SC52932K ↗
29. 10.1016/j.chempr.2018.05.01610.1016/j.chempr.2018.05.016 ↗
30. 10.1073/pnas.203452210010.1073/pnas.2034522100 ↗
31. 10.1073/pnas.87.3.87110.1073/pnas.87.3.871 ↗
32. 10.1016/j.jmb.2005.01.03710.1016/j.jmb.2005.01.037 ↗
33. 10.1073/pnas.051054910310.1073/pnas.0510549103 ↗
34. 10.1021/ja076838510.1021/ja0768385 ↗
35. 10.1126/science.288.5470.140410.1126/science.288.5470.1404 ↗
36. 10.1021/ja06085810.1021/ja060858 ↗
37. 10.1002/anie.20046094310.1002/anie.200460943 ↗
38. 10.1021/ja064044510.1021/ja0640445 ↗
39. 10.1038/nature0368010.1038/nature03680 ↗
40. 10.1074/jbc.M71035120010.1074/jbc.M710351200 ↗
41. 10.1038/s41522-017-0025-210.1038/s41522-017-0025-2 ↗
42. 10.1073/pnas.23259139910.1073/pnas.232591399 ↗
43. 10.1021/ja045600310.1021/ja0456003 ↗
44. 10.1021/ja906528310.1021/ja9065283 ↗
45. 10.1016/j.bmcl.2014.06.05210.1016/j.bmcl.2014.06.052 ↗
46. 10.1016/j.jmb.2016.03.01310.1016/j.jmb.2016.03.013 ↗
47. 10.1038/s41467-017-01424-410.1038/s41467-017-01424-4 ↗
48. 10.1039/D4NR03030C10.1039/D4NR03030C ↗
49. 10.1016/j.sbi.2003.12.00210.1016/j.sbi.2003.12.002 ↗
50. 10.1016/j.jmb.2008.11.00510.1016/j.jmb.2008.11.005 ↗
51. 10.1038/ncomms357510.1038/ncomms3575 ↗
52. 10.1021/bm200216u10.1021/bm200216u ↗
53. 10.1002/ange.20150896810.1002/ange.201508968 ↗
54. 10.1038/s41467-021-22895-610.1038/s41467-021-22895-6 ↗
55. 10.1038/nnano.2011.10210.1038/nnano.2011.102 ↗
56. 10.1021/ja206513r10.1021/ja206513r ↗
57. 10.1038/nnano.2010.5910.1038/nnano.2010.59 ↗
58. 10.1002/advs.20200218210.1002/advs.202002182 ↗
59. 10.1021/ma502264c10.1021/ma502264c ↗
60. 10.1039/C8NR02159G10.1039/C8NR02159G ↗
61. 10.1103/PhysRevLett.107.23810110.1103/PhysRevLett.107.238101 ↗
62. 10.1016/j.polymer.2013.02.02910.1016/j.polymer.2013.02.029 ↗
63. 10.1038/s41594-018-0045-510.1038/s41594-018-0045-5 ↗
64. Case D. A. · 2022
65. 10.1088/1361-648X/aa680e10.1088/1361-648X/aa680e ↗
66. 10.1107/S002188989500704710.1107/S0021889895007047 ↗
67. 10.1039/b922045c10.1039/b922045c ↗
68. 10.1039/C4AN01061B10.1039/C4AN01061B ↗
69. 10.1021/acsomega.4c0683010.1021/acsomega.4c06830 ↗
70. 10.1002/jcc.2003510.1002/jcc.20035 ↗
71. 10.1021/jp973084f10.1021/jp973084f ↗
72. 10.1021/jp003020w10.1021/jp003020w ↗
73. 10.1002/adma.20240619210.1002/adma.202406192 ↗
74. 10.1016/j.giant.2023.10021410.1016/j.giant.2023.100214 ↗
75. Cheng Y. · Angew. Chem., Int. Ed. · 2025
76. 10.1002/advs.20220726910.1002/advs.202207269 ↗
77. 10.1002/adma.20241304910.1002/adma.202413049 ↗
78. 10.1021/acsbiomaterials.7b0018310.1021/acsbiomaterials.7b00183 ↗
79. 10.1038/nnano.2012.6910.1038/nnano.2012.69 ↗
80. 10.1002/adma.20110173310.1002/adma.201101733 ↗
81. 10.1021/nn901127k10.1021/nn901127k ↗
82. 10.1021/acsami.3c1425410.1021/acsami.3c14254 ↗
83. 10.1021/acs.biomac.4c0130510.1021/acs.biomac.4c01305 ↗
84. 10.1088/0031-9112/36/12/02710.1088/0031-9112/36/12/027 ↗
85. 10.1038/nmat504510.1038/nmat5045 ↗
86. 10.1063/1.274258710.1063/1.2742587 ↗
87. 10.1063/1.131724410.1063/1.1317244 ↗
88. 10.1021/nl080704n10.1021/nl080704n ↗
89. 10.1002/adfm.20110301110.1002/adfm.201103011 ↗
90. 10.1021/acsbiomaterials.6b0002110.1021/acsbiomaterials.6b00021 ↗
91. 10.1109/TBME.1974.32438010.1109/TBME.1974.324380 ↗
92. S.Zhang R.Xia T. R.Shrout in2006 IEEE International Symposium on the Applications of Ferroelectrics IEEE Sunset Beach NC USA 2006 pp.1–7.10.1109/ISAF.2006.4349278 ↗
93. 10.1038/ncomms1356610.1038/ncomms13566 ↗
94. 10.1021/jacs.3c0299310.1021/jacs.3c02993 ↗
95. 10.1021/jacs.2c0632110.1021/jacs.2c06321 ↗
96. 10.1038/nature1379210.1038/nature13792 ↗
97. 10.1063/1.496162310.1063/1.4961623 ↗
98. 10.1021/jp960669l10.1021/jp960669l ↗
99. 10.1002/jcc.2105710.1002/jcc.21057 ↗
100. 10.1063/1.47840110.1063/1.478401 ↗