Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. Academic Article uri icon

Overview

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.

publication date

  • December 15, 2016

Research

keywords

  • Calcitonin
  • Phenylalanine

Identity

PubMed Central ID

  • PMC5573999

Scopus Document Identifier

  • 85007197255

Digital Object Identifier (DOI)

  • 10.1002/chem.201604639

PubMed ID

  • 27806188

Additional Document Info

volume

  • 23

issue

  • 9