Toward the synthesis of artificial proteins: The discovery of an amphiphilic helical peptoid assembly
Toward the synthesis of artificial proteins: The discovery of an amphiphilic helical peptoid assembly
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DOI：
10.1016/s1074-5521(02)00140-0
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发表时间：
2002-05-01
影响因子：
--
通讯作者：
Zuckermann, RN
中科院分区：
文献类型：
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作者：
Burkoth, TS;Beausoleil, E;Zuckermann, RN
虽然自然界利用折叠的生物聚合物来实现分子识别和催化，但类似的非生物杂聚物系统很难创造。我们合成并鉴定了能够结合染料的非生物类肽杂聚物。使用组合合成，我们在超高容量珠状支持物上构建了3400个两亲性15-mer类肽库。将各自含有单个类肽序列的单个大珠排列成板，切割，并在水溶液中筛选以定位染料结合杂聚物组装体。再合成和表征表明，确定的螺旋组装的形成，通过尺寸排阻色谱法，圆二色性，和分析超离心判断。受自然界序列变异和自然选择过程的启发，我们发现了罕见的非生物序列特异性杂聚物，它们开始模仿其生物对应物的结构和功能特性。
While nature exploits folded biopolymers to achieve molecular recognition and catalysis, comparable abiological heteropolymer systems have been difficult to create. We synthesized and identified abiological peptoid heteroploymers capable of binding a dye. Using combinatorial synthesis, we constructed a library of 3400 amphiphilic 15-mer peptoids on an ultra-high-capacity beaded support. Individual macrobeads, each containing a single peptoid sequence, were arrayed into plates, cleaved, and screened in aqueous solution to locate dye binding heteropolymer assemblies. Resynthesis and characterization demonstrated the formation of defined helical assemblies as judged by size-exclusion chromatography, circular dichroism, and analytical ultracentrifugation. Inspired by nature's process of sequence variation and natural selection, we identified rare abiological sequence-specific heteropolymers that begin to mimic the structure and functional properties of their biological counterparts.