| Title | Protein β-interfaces as a generic source of native peptide tectons |
| Publication Type | Journal Article |
| Year of Publication | 2013 |
| Authors | Valéry, C., Pandey R., and Gerrard J.A. |
| Journal | Chemical Communications |
| Volume | 49 |
| Issue | 27 |
| Pagination | 2825 - 2827 |
| Date Published | 2013 |
| ISSN | 13597345 (ISSN) |
| Keywords | amino acid sequence, Animals, article, beta lactoglobulin, beta sheet, Carboxy-Lyases, cattle, diaminopimelic acid, dilution, Electron microscopy, Escherichia coli Proteins, Infrared spectroscopy, Lactoglobulins, Models, Molecular, Nanostructures, nonhuman, peptide, Peptide Fragments, peroxiredoxin 3, Peroxiredoxin III, pH, protein, Protein Conformation, Protein Multimerization, protein secondary structure, water |
| Abstract | Motifs of 7-8 amino acids were designed from the β-continuous interfaces of non-related homo-oligomeric proteins. These peptides intrinsically self-assembled into nanoarchitectures in water, while retaining some properties of their parent interfaces, especially reversibility of assembly. These results reveal a novel source of native peptide tectons. © The Royal Society of Chemistry 2013. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84874925930&partnerID=40&md5=d0e9f7c38a3471b07a689a6ca0b5a1d6 |
| DOI | 10.1039/c3cc39052g |
