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

Loading...
Thumbnail Image
Journal Title
Journal ISSN
Volume Title
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
Date
2017-02-10
Major/Subject
Mcode
Degree programme
Language
en
Pages
2051-2058
Series
CHEMISTRY: A EUROPEAN JOURNAL, Volume 23, issue 9
Abstract
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.
Description
Keywords
Amyloid beta-peptides, Aromatic interactions, Crystal structures, Iodination, Peptides
Other note
Citation
Bertolani , A , Pizzi , A , Pirrie , L , Gazzera , L , Morra , G , Meli , M , Colombo , G , Genoni , A , Cavallo , G , Terraneo , G & Metrangolo , P 2017 , ' Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines ' , CHEMISTRY: A EUROPEAN JOURNAL , vol. 23 , no. 9 , pp. 2051-2058 . https://doi.org/10.1002/chem.201604639