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Supramolecular fibrillation of peptide amphiphiles induces environmental responses in aqueous droplets

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  • Richard Booth

    (Universidade de Santiago de Compostela)

  • Ignacio Insua

    (Universidade de Santiago de Compostela)

  • Sahnawaz Ahmed

    (Universidade de Santiago de Compostela)

  • Alicia Rioboo

    (Universidade de Santiago de Compostela)

  • Javier Montenegro

    (Universidade de Santiago de Compostela)

Abstract

One-dimensional (1D) supramolecular polymers are commonly found in natural and synthetic systems to prompt functional responses that capitalise on hierarchical molecular ordering. Despite amphiphilic self-assembly being significantly studied in the context of aqueous encapsulation and autopoiesis, very little is currently known about the physico-chemical consequences and functional role of 1D supramolecular polymerisation confined in aqueous compartments. Here, we describe the different phenomena that resulted from the chemically triggered supramolecular fibrillation of synthetic peptide amphiphiles inside water microdroplets. The confined connection of suitable dormant precursors triggered a physically autocatalysed chemical reaction that resulted in functional environmental responses such as molecular uptake, fusion and chemical exchange. These results demonstrate the potential of minimalistic 1D supramolecular polymerisation to modulate the behaviour of individual aqueous entities with their environment and within communities.

Suggested Citation

  • Richard Booth & Ignacio Insua & Sahnawaz Ahmed & Alicia Rioboo & Javier Montenegro, 2021. "Supramolecular fibrillation of peptide amphiphiles induces environmental responses in aqueous droplets," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26681-2
    DOI: 10.1038/s41467-021-26681-2
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    References listed on IDEAS

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    Cited by:

    1. Ayan Chatterjee & Surashree Goswami & Raushan Kumar & Janmejay Laha & Dibyendu Das, 2024. "Emergence of a short peptide based reductase via activation of the model hydride rich cofactor," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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