Protein nanofibril design via manipulation of hydrogen bonds
How the structure of fibril-forming peptides influences the material and structural characteristics of their resultant assemblies remains an open question. Here, aliphatic to aromatic amino acid substitution in such peptides is shown to have little effect on the tendency to form amyloid-like fibrils...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2021-05-01
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| Series: | Communications Chemistry |
| Online Access: | https://doi.org/10.1038/s42004-021-00494-2 |
| Summary: | How the structure of fibril-forming peptides influences the material and structural characteristics of their resultant assemblies remains an open question. Here, aliphatic to aromatic amino acid substitution in such peptides is shown to have little effect on the tendency to form amyloid-like fibrils, but instead alters the pathway by which they form and the mechanical properties of peptide supramolecular assemblies. |
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| ISSN: | 2399-3669 |