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Protein Recognition by Functionalized Sulfonatocalix[4]arenes.

Aishling M DoolanMartin L RenniePeter B Crowley
Published in: Chemistry (Weinheim an der Bergstrasse, Germany) (2017)
The interactions of two mono-functionalized sulfonatocalix[4]arenes with cytochrome c were investigated by structural and thermodynamic methods. The replacement of a single sulfonate with either a bromo or a phenyl substituent resulted in altered recognition of cytochrome c as evidenced by X-ray crystallography. The bromo-substituted ligand yielded a new binding mode in which a self-encapsulated calixarene dimer contributed to crystal packing. This ligand also formed a weak halogen bond with the protein. The phenyl-substituted ligand was bound to Lys4 of cytochrome c, in a 1.7 Å resolution crystal structure. A dimeric packing arrangement mediated by ligand-ligand contacts in the crystal suggested a possible assembly mechanism. The different protein recognition properties of these calixarenes are discussed.
Keyphrases
  • crystal structure
  • binding protein
  • protein protein
  • molecular docking
  • amino acid
  • high resolution
  • mass spectrometry
  • atomic force microscopy
  • solid state
  • dual energy