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- W2000960287 abstract "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." @default.
- W2000960287 created "2016-06-24" @default.
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- W2000960287 date "2013-01-01" @default.
- W2000960287 modified "2023-10-13" @default.
- W2000960287 title "Lamination and spherulite-like compaction of a hormone’s native amyloid-like nanofibrils: spectroscopic insights into key interactions" @default.
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- W2000960287 doi "https://doi.org/10.1039/c3fd00054k" @default.
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