Random heteropolymers preserve protein function in foreign environments

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Science  16 Mar 2018:
Vol. 359, Issue 6381, pp. 1239-1243
DOI: 10.1126/science.aao0335

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Mimicking the designs found in proteins

Natural proteins combine a range of useful features, including chemical diversity, the ability to rapidly switch between preprogrammed shapes, and a hierarchy of structures. Panganiban et al. designed random copolymers with polar and nonpolar groups, using many of the features found in proteins (see the Perspective by Alexander-Katz and Van Lehn). Their structures could serve as “broad spectrum” surfactants, able to promote the solubilization of proteins in organic solvents and help preserve the functionality of proteins in aqueous environments.

Science, this issue p. 1239; see also p. 1216


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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