beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers
beta-peptide foldamers: Robust Helix formation in a new family of beta-amino acid oligomers
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DOI：
10.1021/ja963290l
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发表时间：
1996-12-25
影响因子：
15
通讯作者：
Gellman, SH
中科院分区：
文献类型：
--
作者：
Appella, DH;Christianson, LA;Gellman, SH
化学家长期以来一直试图将生物催化和识别的力量外推到合成系统中。这些努力主要集中在低分子量催化剂和受体上; 1-3然而，生物系统本身几乎完全依赖于聚合物、蛋白质和RNA来执行复杂的化学功能。蛋白质和RNA具有独特的能力，能够采用紧凑、有序的构象，并且特异性折叠提供了构成“活性位点”的官能团的精确空间取向。这些特征表明，识别具有离散和可预测的折叠倾向的新聚合物主链（“折叠体”）将为设计具有独特能力的分子机器提供基础。折叠体方法补充了当前将非天然性质设计到多肽和多核苷酸中的努力。4-7创建折叠体的第一步是鉴定具有明确的二级结构偏好的聚合物主链。8-18在这里，我们描述了一个新的聚酰胺家族（1-5），强烈支持一个特定的螺旋二级结构，这最终应该作为一个稳定的三级结构的构建块。
Chemists have long sought to extrapolate the power of biological catalysis and recognition to synthetic systems. These efforts have focused largely on low molecular weight catalysts and receptors; 1-3 however, biological systems themselves rely almost exclusively on polymers, proteins and RNA, to perform complex chemical functions. Proteins and RNA are unique in their ability to adopt compact, well-ordered conformations, and specific folding provides precise spatial orientation of the functional groups that comprise the “active site”. These features suggest that identification of new polymer backbones with discrete and predictable folding propensities (“foldamers”) will provide a basis for design of molecular machines with unique capabilities. The foldamer approach complements current efforts to design unnatural properties into polypeptides and polynucleotides. 4-7 The first step in creating a foldamer is to identify polymeric backbones with well-defined secondary structural preferences. 8-18 Here we describe a new polyamide family (1-5) that strongly favors a specific helical secondary structure, which should ultimately serve as a building block for stable tertiary structures.