Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 23, Issue 9, Pages 2051-2058Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201604639
Keywords
amyloid beta-peptides; aromatic interactions; crystal structures; iodination; peptides
Categories
Funding
- European Research Council [ERC-2012-StG_20111012 FOLDHALO, 307108]
- European Research Council (ERC) [307108] Funding Source: European Research Council (ERC)
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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-beta 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.
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