Although intensively studied, the high-resolution crystal structure of the peptide DFNKF, the core-segment of human calcitonin, has never been described. Here we report how the use of iodination as a strategy to promote crystallisation and facilitate phase determination, allowed us to solve, for the first time, the single-crystal X-ray structure of a DFNKF derivative. Computational studies suggest that both the iodinated and the wild-type peptides populate very similar conformations. Furthermore, the conformer found in the solid-state structure is one of the most populated in solution, making the crystal structure a reliable model for the peptide in solution. The crystal structure of DFNKF(I) confirms the overall features of the amyloid cross-β spine and highlights how aromatic-aromatic interactions are important structural factors in the self-assembly of this peptide. A detailed analysis of such interactions is reported.
- Amyloid beta-peptides
- Aromatic interactions
- Crystal structures
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Bertolani, A. (Contributor), Cavallo, G. (Contributor), Colombo, G. (Contributor), Gazzera, L. (Contributor), Genoni, A. (Contributor), Meli, M. (Contributor), Metrangolo, P. (Contributor), Morra, G. (Contributor), Pirrie, L. (Contributor), Pizzi, A. (Contributor) & Terraneo, G. (Contributor), Cambridge Crystallographic Data Centre , 1 Jan 2017