Biomimetic Hybrid Nanocontainers with Selective Permeability

Chemistry plays a crucial role in creating synthetic analogues of biomacromolecular structures. Of particular scientific and technological interest are biomimetic vesicles that are inspired by natural membrane compartments and organelles but avoid their drawbacks, such as membrane instability and li...

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Bibliographic Details
Published in:Angewandte Chemie International Edition Vol. 55; no. 37; pp. 11106 - 11109
Main Authors: Messager, Lea, Burns, Jonathan R., Kim, Jungyeon, Cecchin, Denis, Hindley, James, Pyne, Alice L. B., Gaitzsch, Jens, Battaglia, Giuseppe, Howorka, Stefan
Format: Journal Article
Language:English
Published: Germany Blackwell Publishing Ltd 05-09-2016
Wiley Subscription Services, Inc
John Wiley and Sons Inc
Edition:International ed. in English
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Summary:Chemistry plays a crucial role in creating synthetic analogues of biomacromolecular structures. Of particular scientific and technological interest are biomimetic vesicles that are inspired by natural membrane compartments and organelles but avoid their drawbacks, such as membrane instability and limited control over cargo transport across the boundaries. In this study, completely synthetic vesicles were developed from stable polymeric walls and easy‐to‐engineer membrane DNA nanopores. The hybrid nanocontainers feature selective permeability and permit the transport of organic molecules of 1.5 nm size. Larger enzymes (ca. 5 nm) can be encapsulated and retained within the vesicles yet remain catalytically active. The hybrid structures constitute a new type of enzymatic nanoreactor. The high tunability of the polymeric vesicles and DNA pores will be key in tailoring the nanocontainers for applications in drug delivery, bioimaging, biocatalysis, and cell mimicry. Functional hybrid nanocontainers composed of polymersomes (purple/gray) and DNA nanopores (blue) exhibit size‐selective permeability and permit the transport of enzyme substrates and products through the DNA nanopores while bioactive encapsulated enzymes (green) are retained.
Bibliography:EPSRC - No. EP/N009282/1; No. EP/M506448/1
istex:2068FAB1257C6C639181E8F9C4A437ED3F0C0CC3
ark:/67375/WNG-V152G82F-1
BBSRC - No. BB/M012700/1; No. BB/M025373/1; No. BB/N017331/1; No. ERC-MEViC-STG-2011
ArticleID:ANIE201604677
These authors contributed equally to this work.
ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201604677