Protein-macrocycle framework engineering: supramolecular copolymerisation with two disparate calixarenes

Niamh M. Mockler, Sylvain Engilberge, Martin L. Rennie, Colin L. Raston, Peter B. Crowley

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Water soluble calixarenes are versatile mediators of protein assembly, including the fabrication of crystalline frameworks. Here, we report the X-ray crystal structure of cytochrome c (cytc) co-crystallised with two different calixarenes: phosphonato-calix[6]arene (pclx6) and sulfonato-calix[8]arene (sclx8). Each calixarene type acts as an independent molecular glue that mediates cytc dimers within the crystal. The calixarene-mediated dimers combine to yield chains of cytc-sclx8 -cytc-pclx6-pclx6 repeating units. These supramolecular copolymer units pack together, via a protein-protein interface, to yield a porous dendrite-like assembly. Interestingly, the tri-component framework has features in common with previously reported structures of cytc in complex with pclx6 or sclx8. Known protein-calixarene ‘building blocks’ combine in novel ways to yield the tri-component assembly, highlighting the versatility of calixarene molecular glues in protein crystal engineering.

    Original languageEnglish
    Number of pages7
    JournalSupramolecular Chemistry
    Early online date6 Jun 2021
    DOIs
    Publication statusE-pub ahead of print - 6 Jun 2021

    Keywords

    • Conformation
    • crystal engineering
    • molecular glue
    • recognition
    • self-assembly

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