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

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.

SUBMITTER: Bertolani A 

PROVIDER: S-EPMC5573999 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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

Bertolani Arianna A   Pizzi Andrea A   Pirrie Lisa L   Gazzera Lara L   Morra Giulia G   Meli Massimiliano M   Colombo Giorgio G   Genoni Alessandro A   Cavallo Gabriella G   Terraneo Giancarlo G   Metrangolo Pierangelo P  

Chemistry (Weinheim an der Bergstrasse, Germany) 20161215 9

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  ...[more]

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