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Random heteropolymers preserve protein function in foreign environments
Science ( IF 44.7 ) Pub Date : 2018-03-15 , DOI: 10.1126/science.aao0335
Brian Panganiban 1 , Baofu Qiao 2 , Tao Jiang 1 , Christopher DelRe 1 , Mona M. Obadia 3 , Trung Dac Nguyen 2 , Anton A. A. Smith 1 , Aaron Hall 1 , Izaac Sit 1 , Marquise G. Crosby 4 , Patrick B. Dennis 4 , Eric Drockenmuller 3 , Monica Olvera de la Cruz 2, 5 , Ting Xu 1, 6, 7, 8
Affiliation  

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 Statistically random heteropolymers are designed using pattern analysis of protein sequence and surface chemistry. 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.

中文翻译:

随机杂聚物在外来环境中保持蛋白质功能

模仿在蛋白质中发现的设计 天然蛋白质结合了一系列有用的特征,包括化学多样性、在预编程形状之间快速切换的能力以及结构层次。潘加尼班等。使用蛋白质中发现的许多特征设计了具有极性和非极性基团的无规共聚物(参见 Alexander-Katz 和 Van Lehn 的观点)。它们的结构可以作为“广谱”表面活性剂,能够促进蛋白质在有机溶剂中的溶解,并有助于保持蛋白质在水性环境中的功能。科学,这个问题 p。1239; 另见第。1216 统计无规杂聚物是使用蛋白质序列和表面化学的模式分析设计的。将活性蛋白质成功掺入合成聚合物可能会产生一类新的材料,其功能仅存在于生命系统中。然而,蛋白质很少在适合聚合物加工的条件下起作用。在分析蛋白质序列趋势和蛋白质表面特征化学模式的基础上,我们设计了四单体随机杂聚物来模拟本质上无序的蛋白质,用于在非天然环境中溶解和稳定蛋白质。杂聚物具有优化的组成和统计单体分布,能够无细胞合成具有适当蛋白质折叠的膜蛋白,用于运输和含有酶的塑料用于毒素生物修复。控制杂聚物中的统计单体分布,
更新日期:2018-03-15
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