Interfacial assembly of protein–polymer nano-conjugates into stimulus-responsive biomimetic protocells

Xin Huang, Mei Li, David C. Green, David S. Williams, Avinash J. Patil and Stephen Mann ()
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Xin Huang: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol
Mei Li: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol
David C. Green: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol
David S. Williams: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol
Avinash J. Patil: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol
Stephen Mann: Centre for Organized Matter Chemistry, School of Chemistry, University of Bristol

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract The mechanism of spontaneous assembly of microscale compartments is a central question for the origin of life, and has technological repercussions in diverse areas such as materials science, catalysis, biotechnology and biomedicine. Such compartments need to be semi-permeable, structurally robust and capable of housing assemblages of functional components for internalized chemical transformations. In principle, proteins should be ideal building blocks for the construction of membrane-bound compartments but protein vesicles with cell-like properties are extremely rare. Here we present an approach to the interfacial assembly of protein-based micro-compartments (proteinosomes) that are delineated by a semi-permeable, stimulus-responsive, enzymatically active, elastic membrane consisting of a closely packed monolayer of conjugated protein–polymer building blocks. The proteinosomes can be dispersed in oil or water, thermally cycled to temperatures of 70 °C, and partially dried and re-inflated without loss of structural integrity. As a consequence, they exhibit protocellular properties such as guest molecule encapsulation, selective permeability, gene-directed protein synthesis and membrane-gated internalized enzyme catalysis.

Date: 2013
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DOI: 10.1038/ncomms3239

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