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Related Experiment Videos

Protein Dimerization on a Phosphonated Calix[6]arene Disc.

Martin L Rennie1, Aishling M Doolan1, Colin L Raston2

  • 1School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland.

Angewandte Chemie (International Ed. in English)
|April 14, 2017
PubMed
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A novel supramolecular assembly forms between cytochrome c and p-phosphonatocalix[6]arene (pclx6), creating a protein dimer. This interaction, mediated by the pclx6 dimeric disc, reveals a specific binding site crucial for complex formation.

Area of Science:

  • Supramolecular chemistry
  • Biophysical chemistry
  • Structural biology

Background:

  • Cytochrome c is a vital protein involved in electron transport.
  • Calixarenes are macrocyclic compounds with diverse applications.
  • Understanding protein-macrocycle interactions is key for biomaterials and drug design.

Purpose of the Study:

  • To investigate the complex formation between cationic cytochrome c and poly-anionic p-phosphonatocalix[6]arene (pclx6).
  • To elucidate the structural basis and binding characteristics of this protein-calixarene complex.

Main Methods:

  • X-ray crystallography (1.8 Å resolution) for structural determination.
  • Size-exclusion chromatography with multi-angle light scattering (SEC-MALS) for solution assembly analysis.
Keywords:
cytochrome clysine recognitionpolyanionsself-assemblystructure elucidation

Related Experiment Videos

  • Nuclear Magnetic Resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC) for binding studies.

    • Main Results:

    • A crystal structure revealed a dimeric disc of pclx6 mediating a symmetric cytochrome c dimer.
    • The pclx6 disc (1.5 nm diameter) masks ~360 Ų of the protein surface, with key contacts involving lysines.
    • Solution studies confirmed supramolecular assembly, and ITC/NMR determined a low micromolar dissociation constant (Kd).

    Conclusions:

    • P-phosphonatocalix[6]arene (pclx6) forms a well-defined complex with cytochrome c, unlike smaller analogs.
    • The larger pclx6 acts as a specific mediator, facilitating cytochrome c dimerization through a single binding site.
    • This study provides insights into supramolecular assembly driven by protein-macrocycle interactions.