Self-assembling amphiphiles for construction of protein molecular architecture
Self-assembling amphiphiles for construction of protein molecular architecture
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DOI：
10.1021/ja9627656
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发表时间：
1996-12-18
影响因子：
15
通讯作者：
Fields, GB
中科院分区：
文献类型：
--
作者：
Yu, YC;Berndt, P;Fields, GB
肽与胶原模型的头部基团和二烷基链尾的两亲物已被合成，并显示出自组装成高度有序的聚Pro II一样的三螺旋结构时，溶解在水亚相。这种自组装过程的证据已经从以下方面获得：（a）将稳定的肽-两亲物单层压缩到与三螺旋区域相当的分子区域，（B）三螺旋特征的圆二色性光谱和熔化曲线，以及（c）指示在低温下稳定的三螺旋结构和在高温下熔化的三螺旋的二维NMR光谱。肽-两亲物中胶原蛋白样结构的热稳定性（Δ T-m = 15-20 ℃）显著高于没有脂化的肽。由疏水尾部驱动的组装过程可以提供使用最低限度的基于肽的方法来创建明确定义的蛋白质分子结构的一般方法。
Peptide-amphiphiles with collagen-model head groups and dialkyl chain tails have been synthesized and shown to self-assemble into highly ordered polyPro II like triple-helical structures when dissolved in aqueous subphases. Evidence for this self-assembly process has been obtained from (a) compression of stable peptide-amphiphile monolayers to molecular areas comparable with triple-helical areas, (b) circular dichroism spectra and melting curves characteristic of triple-helices, and (c) two-dimensional NMR spectra indicative of stable triple-helical structure at low temperatures and melted triple-helices at high temperatures. The thermal stability of the collagen-like structure in the peptide-amphiphile is substantially higher (Delta T-m = 15-20 degrees C) than that of peptides without lipidation. The assembly process driven by the hydrophobic tail may provide a general method for creating well-defined protein molecular architecture using a minimalist peptide-based approach.