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Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines

Abstract : Althoughi ntensively studied, the high-resolution crystal structure of the peptide DFNKF,t he core-segment of human calcitonin, hasn ever been described. Here we report how the use of iodination as as trategy to promote crystalli-sation andf acilitate phased etermination,a llowed 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 similarc onformations. Furthermore, the conformer found in the solid-state structure is one of the mostpopulat-ed in solution,m aking the crystal structure ar eliable model for the peptide in solution. The crystal structure of DFNKF(I) confirmst he overall features of the amyloid cross-b spine and highlights how aromatic-aromatic interactions are im-portants tructural factors in the self-assembly of this peptide. Adetailed analysis of such interactions is reported.
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Arianna Bertolani, Andrea Pizzi, Lisa Pirrie, Lara Gazzera, Giulia Morra, et al.. Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. Chemistry - A European Journal, Wiley-VCH Verlag, 2017, 23 (9), pp.2051-2058. ⟨10.1002/chem.201604639⟩. ⟨hal-02196477⟩

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