Lamination and spherulite-like compaction of a hormone's native amyloid-like nanofibrils: spectroscopic insights into key interactions
| Autor: | Sophie Lecomte, Roland Cherif-Cheikh, Wilmar van Grondelle, Carmen López-Iglesias, Céline Valéry, Maïté Paternostre, Jose-Maria Manero |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Amyloid Chemistry Spectrum Analysis Molecular Sequence Data Nanofibers Peptide Fibrillogenesis Protein aggregation Hormones law.invention symbols.namesake Crystallography Spherulite law Nanofiber Biophysics symbols Microscopy Electron Scanning Amino Acid Sequence Physical and Theoretical Chemistry Electron microscope Raman spectroscopy |
| Zdroj: | Faraday discussions. 166 |
| ISSN: | 1359-6640 |
| Popis: | The native hierarchical self-assembly process of natural somatostatin-14, a highly aromatic and charged peptide hormone involved in various inhibitory functions, was investigated mainly using vibrational spectroscopy (ATR-FTIR and Raman scattering) combined with electron microscopy. Generic kinetic features of amyloid fibrillogenesis were confirmed for the somatostatin-14 case, together with new insights into key interactions involved in the further hierarchical assembly of the somatostatin-14 nanofibrils into i) laterally associated nanofibers and ii) spherulite-like amyloid droplets resulting from the compaction of the nanofibers. In particular, the key role of aromatic side-chains in both fibrillogenesis and the association of the nanofibrils into higher order structures could be followed. It is proposed that the compaction propensity of the somatostatin-14 nanofibrils is relevant to the current hypothesis of the biological function of hormone self-assembly processes: hormone storage inside secretory granules. |
| Databáze: | OpenAIRE |
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