| Autor: |
van Grondelle W; Ipsen Pharma, Carrer Laureà Miró 395, Sant Feliu de Llobregat, 08980 Barcelona, Spain., Iglesias CL, Coll E, Artzner F, Paternostre M, Lacombe F, Cardus M, Martinez G, Montes M, Cherif-Cheikh R, Valéry C |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of structural biology [J Struct Biol] 2007 Nov; Vol. 160 (2), pp. 211-23. Date of Electronic Publication: 2007 Aug 23. |
| DOI: |
10.1016/j.jsb.2007.08.006 |
| Abstrakt: |
Natural Somatostatin-14 is a small cyclic neuropeptide hormone with broad inhibitory effects on endocrine secretions. Here we show that natural Somatostatin-14 spontaneously self-assembles in water and in 150 mM NaCl into liquid crystalline nanofibrils, which follow characteristic structural features of amyloid fibrils. These non-covalent highly stable structures are based on the Somatostatin native backbone conformation and are formed under non-denaturing conditions. Our results support the hypothesis that self-assembly into amyloid fibrils is a generic property of the polypeptide chain under appropriate conditions. Given recent advances on the mechanisms of biological storage and sorting modes of peptide/protein hormones into secretory granules, we propose that Somatostatin-14 fibrillation could be relevant to the regulated secretion pathway of this neuropeptide hormone. Such a hypothesis is consistent with the emerging concept of the existence of non-disease related but functional amyloids. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
Full Text from ScienceDirect