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

Chemistry

Laboratory of Nanostructured Fluorinated Materials (NFMLab), Department of Chemistry, Materials, and Chemical Engineering "Giulio Natta", Politecnico di Milano, Via L. Mancinelli 7, 20131, Milano, Italy.

Published: February 2017

AI Article Synopsis

  • Researchers successfully determined the high-resolution crystal structure of the peptide DFNKF, a component of human calcitonin, using iodination to aid in crystallization.
  • The study found that both iodinated and wild-type peptides exhibit similar conformations, with the crystal structure representing one of the most common forms seen in solution.
  • The crystal structure highlights the significance of aromatic-aromatic interactions in the peptide's self-assembly, reinforcing the structural understanding of amyloid formations.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5573999PMC
http://dx.doi.org/10.1002/chem.201604639DOI Listing

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