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

被引:410
作者
Huang, Xin [1 ]
Li, Mei [1 ]
Green, David C. [1 ]
Williams, David S. [1 ]
Patil, Avinash J. [1 ]
Mann, Stephen [1 ]
机构
[1] Univ Bristol, Sch Chem, Ctr Organized Matter Chem, Bristol BS8 1TS, Avon, England
来源
NATURE COMMUNICATIONS | 2013年 / 4卷
基金
英国工程与自然科学研究理事会;
关键词
SELF-REPRODUCTION; CAPSULES; VESICLES; MICROCAPSULES; COLLOIDOSOMES; PERMEABILITY; COMPLEX; CELLS;
D O I
10.1038/ncomms3239
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 semipermeable, 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 degrees 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.
引用
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页数:9
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