Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide
Squid sucker ring teeth (SRT) have emerged as a promising protein-only, thermoplastic biopolymer with an increasing number of biomedical and engineering applications demonstrated in recent years. SRT is a supra-molecular network whereby a flexible, amorphous matrix is mechanically reinforced by nano...
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2020
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| Online Access: | https://hdl.handle.net/10356/143593 |
| _version_ | 1826124017584570368 |
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| author | Sanchez-Ferrer, Antoni Adamcik, Jozef Handschin, Stephan Hiew, Shu Hui Miserez, Ali Mezzenga, Raffaele |
| author2 | School of Materials Science and Engineering |
| author_facet | School of Materials Science and Engineering Sanchez-Ferrer, Antoni Adamcik, Jozef Handschin, Stephan Hiew, Shu Hui Miserez, Ali Mezzenga, Raffaele |
| author_sort | Sanchez-Ferrer, Antoni |
| collection | NTU |
| description | Squid sucker ring teeth (SRT) have emerged as a promising protein-only, thermoplastic biopolymer with an increasing number of biomedical and engineering applications demonstrated in recent years. SRT is a supra-molecular network whereby a flexible, amorphous matrix is mechanically reinforced by nanoconfined β-sheets. The building blocks for the SRT network are a family of suckerin proteins that share a common block copolymer architecture consisting of amorphous domains intervened by smaller, β-sheet forming modules. Recent studies have identified the peptide A1H1 (peptide sequence AATAVSHTTHHA) as one of the most abundant β-sheet forming domains within the suckerin protein family. However, we still have little understanding of the assembly mechanisms by which the A1H1 peptide may assemble into its functional load-bearing domains. In this study, we conduct a detailed self-assembly study of A1H1 and show that the peptide undergoes β-strands-driven elongation into amyloid-like fibrils with a rich polymorphism. The nanostructure of the fibrils was elucidated by small and wide-angle X-ray scattering (SAXS and WAXS) and atomic force microscopy (AFM). The presence of His-rich and Ala-rich segments results in an amphiphilic behavior and drives its assembly into fibrillar supramolecular chiral aggregates with helical ribbon configuration in solution, with the His-rich region exposed to the solvent molecules. Upon increase in concentration, the fibrils undergo gel formation, while preserving the same mesoscopic features. This complex phase behavior suggests that the repeat peptide modules of suckerins may be manipulated beyond their native biological environment to produce a wider variety of self-assembled amyloid-like nanostructures. |
| first_indexed | 2024-10-01T06:13:47Z |
| format | Journal Article |
| id | ntu-10356/143593 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:13:47Z |
| publishDate | 2020 |
| record_format | dspace |
| spelling | ntu-10356/1435932020-09-14T01:08:48Z Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide Sanchez-Ferrer, Antoni Adamcik, Jozef Handschin, Stephan Hiew, Shu Hui Miserez, Ali Mezzenga, Raffaele School of Materials Science and Engineering School of Biological Sciences Engineering::Materials Science::Biological sciences Self-assembly Peptide Squid sucker ring teeth (SRT) have emerged as a promising protein-only, thermoplastic biopolymer with an increasing number of biomedical and engineering applications demonstrated in recent years. SRT is a supra-molecular network whereby a flexible, amorphous matrix is mechanically reinforced by nanoconfined β-sheets. The building blocks for the SRT network are a family of suckerin proteins that share a common block copolymer architecture consisting of amorphous domains intervened by smaller, β-sheet forming modules. Recent studies have identified the peptide A1H1 (peptide sequence AATAVSHTTHHA) as one of the most abundant β-sheet forming domains within the suckerin protein family. However, we still have little understanding of the assembly mechanisms by which the A1H1 peptide may assemble into its functional load-bearing domains. In this study, we conduct a detailed self-assembly study of A1H1 and show that the peptide undergoes β-strands-driven elongation into amyloid-like fibrils with a rich polymorphism. The nanostructure of the fibrils was elucidated by small and wide-angle X-ray scattering (SAXS and WAXS) and atomic force microscopy (AFM). The presence of His-rich and Ala-rich segments results in an amphiphilic behavior and drives its assembly into fibrillar supramolecular chiral aggregates with helical ribbon configuration in solution, with the His-rich region exposed to the solvent molecules. Upon increase in concentration, the fibrils undergo gel formation, while preserving the same mesoscopic features. This complex phase behavior suggests that the repeat peptide modules of suckerins may be manipulated beyond their native biological environment to produce a wider variety of self-assembled amyloid-like nanostructures. 2020-09-14T01:08:48Z 2020-09-14T01:08:48Z 2018 Journal Article Sanchez-Ferrer, A., Adamcik, J., Handschin, S., Hiew, S. H., Miserez, A., & Mezzenga, R. (2018). Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide. ACS Nano, 12(9), 9152-9161. doi:10.1021/acsnano.8b03582 1936-086X https://hdl.handle.net/10356/143593 10.1021/acsnano.8b03582 30106557 9 12 9152 9161 en ACS Nano © 2018 American Chemical Society. All rights reserved. |
| spellingShingle | Engineering::Materials Science::Biological sciences Self-assembly Peptide Sanchez-Ferrer, Antoni Adamcik, Jozef Handschin, Stephan Hiew, Shu Hui Miserez, Ali Mezzenga, Raffaele Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title | Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title_full | Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title_fullStr | Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title_full_unstemmed | Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title_short | Controlling supramolecular chiral nanostructures by self-assembly of a biomimetic β-sheet-rich amyloidogenic peptide |
| title_sort | controlling supramolecular chiral nanostructures by self assembly of a biomimetic β sheet rich amyloidogenic peptide |
| topic | Engineering::Materials Science::Biological sciences Self-assembly Peptide |
| url | https://hdl.handle.net/10356/143593 |
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