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Protein assembly mediated by sulfonatocalix[4]arene
Róise E McGovern1, Andrew A McCarthy, Peter B Crowley
1School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland. peter.crowley@nuigalway.ie.
Chemical Communications (Cambridge, England)
|July 29, 2014
Summary
Crystal structures reveal how lysozyme proteins assemble into linear chains. These protein chains are linked by p-sulfonato-calix[4]arene (sclx4), with specific interactions involving Arg128 and a complex of sclx4, Mg(2+), and polyethylene glycol.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Lysozyme is a key enzyme in innate immunity.
- Supramolecular assemblies can form through protein-ligand interactions.
- Calixarenes are versatile host molecules with potential biological applications.
Purpose of the Study:
- To elucidate the structural basis of lysozyme assembly mediated by p-sulfonato-calix[4]arene (sclx4).
- To characterize the specific interactions between lysozyme, sclx4, and other co-crystallized molecules.
Main Methods:
- X-ray crystallography was employed to determine the high-resolution structure of the lysozyme-sclx4 complex.
- Detailed structural analysis was performed to identify key binding interfaces and molecular interactions.
Main Results:
- A linear assembly of lysozyme tetramers was observed, mediated by sclx4.
- Specific interactions include the encapsulation of the C-terminal Arg128 residue of lysozyme by sclx4.
- An intricate ternary complex involving sclx4, Mg(2+), and a polyethylene glycol fragment bound to the protein was identified.
Conclusions:
- p-sulfonato-calix[4]arene acts as a molecular glue, directing the assembly of lysozyme into higher-order structures.
- The identified interactions provide insights into protein-ligand complex formation and potential applications in biomaterials or drug delivery.
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