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Sequence-selective encapsulation and protection of long peptides by a self-assembled FeII8L6 cubic cage

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  • Jesús Mosquera

    (University of Cambridge)

  • Bartosz Szyszko

    (University of Cambridge)

  • Sarah K. Y. Ho

    (University of Cambridge)

  • Jonathan R. Nitschke

    (University of Cambridge)

Abstract

Self-assembly offers a general strategy for the preparation of large, hollow high-symmetry structures. Although biological capsules, such as virus capsids, are capable of selectively recognizing complex cargoes, synthetic encapsulants have lacked the capability to specifically bind large and complex biomolecules. Here we describe a cubic host obtained from the self-assembly of FeII and a zinc-porphyrin-containing ligand. This cubic cage is flexible and compatible with aqueous media. Its selectivity of encapsulation is driven by the coordination of guest functional groups to the zinc porphyrins. This new host thus specifically encapsulates guests incorporating imidazole and thiazole moieties, including drugs and peptides. Once encapsulated, the reactivity of a peptide is dramatically altered: encapsulated peptides are protected from trypsin hydrolysis, whereas physicochemically similar peptides that do not bind are cleaved.

Suggested Citation

  • Jesús Mosquera & Bartosz Szyszko & Sarah K. Y. Ho & Jonathan R. Nitschke, 2017. "Sequence-selective encapsulation and protection of long peptides by a self-assembled FeII8L6 cubic cage," Nature Communications, Nature, vol. 8(1), pages 1-6, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14882
    DOI: 10.1038/ncomms14882
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