Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry

Xiao Ming Zhou, Ulyana Shimanovich, Therese W. Herling, Si Wu, Christopher M. Dobson, Tuomas P.J. Knowles, Sarah Perrett

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

Amyloid fibrils represent a generic class of protein structure associated with both pathological states and with naturally occurring functional materials. This class of protein nanostructure has recently also emerged as an excellent foundation for sophisticated functional biocompatible materials including scaffolds and carriers for biologically active molecules. Protein-based materials offer the potential advantage that additional functions can be directly incorporated via gene fusion producing a single chimeric polypeptide that will both self-assemble and display the desired activity. To succeed, a chimeric protein system must self-assemble without the need for harsh triggering conditions which would damage the appended functional protein molecule. However, the micrometer to nanoscale patterning and morphological control of protein-based nanomaterials has remained challenging. This study demonstrates a general approach for overcoming these limitations through the microfluidic generation of enzymatically active microgels that are stabilized by amyloid nanofibrils. The use of scaffolds formed from biomaterials that self-assemble under mild conditions enables the formation of catalytic microgels while maintaining the integrity of the encapsulated enzyme. The enzymatically active microgel particles show robust material properties and their porous architecture allows diffusion in and out of reactants and products. In combination with microfluidic droplet trapping approaches, enzymatically active microgels illustrate the potential of self-assembling materials for enzyme immobilization and recycling, and for biological flow-chemistry. These design principles can be adopted to create countless other bioactive amyloid-based materials with diverse functions.

Original languageEnglish
Pages (from-to)5772-5781
Number of pages10
JournalACS Nano
Volume9
Issue number6
DOIs
StatePublished - 23 Jun 2015
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2015 American Chemical Society.

Funding

FundersFunder number
National Natural Science Foundation of China31100564, 31110103914, 31070656
Biotechnology and Biological Sciences Research CouncilBB/J002119/1

    Keywords

    • Ure2
    • alkaline phosphatase
    • amyloid fibrils
    • enzymatic microgel
    • microfluidics

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