Journal
SCIENCE
Volume 359, Issue 6381, Pages 1239-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aao0335
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Funding
- U.S. Department of Defense (DOD), Army Research Office [W911NF-13-1-0232]
- Department of Energy [DE-FG02-08ER46539]
- Sherman Fairchild Foundation
- Auvergne-Rhone-Alpes region
- Danish Council for Independent Research [DFF-5054-00215]
- Dreyfus foundation via Camille-Dreyfus Teacher-Scholar Award
- Fulbright foundation
- Miller Institute
- DOD through the National Defense Science and Engineering Graduate Fellowship (NDSEG) Program
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The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials.
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