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首页> 外文期刊>Chemistry: A European journal >Sheet-like assemblies of charged amphiphilic α/β-peptides at the air-water interface
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Sheet-like assemblies of charged amphiphilic α/β-peptides at the air-water interface

机译：空气-水界面的带电荷两亲性α/β肽的片状组件

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There is growing interest in the design of molecules that undergo predictable self-assembly. Bioinspired oligomers with well-defined conformational propensities are attractive from this perspective, since they can be constructed from diverse building blocks, and self-assembly can be directed by the identities and sequence of the subunits. Here we describe the structure of monolayers formed at the air-water interface by amphiphilic α/β-peptides with 1:1 alternation of α- and β-amino acid residues along the backbone. Two of the α/β-peptides, one a dianion and the other a dication, were used to determine differences between self-assemblies of the net negatively and positively charged oligomers. Two additional α/β-peptides, both zwitterionic, were designed to favor assembly in a 1:1 molar ratio mixture with parallel orientation of neighboring strands. Monolayers formed by these α/β-peptides at the air-water interface were characterized by surface pressure-area isotherms, grazing incidence X-ray diffraction (GIXD), atomic force microscopy and ATR-FTIR. GIXD data indicate that the α/β-peptide assemblies exhibited diffraction features similar to those of β-sheet-forming α-peptides. The diffraction data allowed the construction of a detailed model of an antiparallel α/β-peptide sheet with a unique pleated structure. One of the α/β-peptide assemblies displayed high stability, unparalleled among previously studied assemblies of α-peptides. ATR-FTIR data suggest that the 1:1 mixture of zwitterionic α/β-peptides assembled in a parallel arrangement resembling that of a typical parallel β-sheet secondary structure formed by α-peptides. This study establishes guidelines for design of amphiphilic α/β-peptides that assemble in a predictable manner at an air-water interface, with control of interstrand orientation through manipulation of Coulombic interactions along the backbone.
机译：人们对可预测的自组装分子的设计越来越感兴趣。从这个角度来看，具有明确构象倾向的生物启发型低聚物具有吸引力，因为它们可以由多种结构单元构建，并且可以通过亚基的身份和序列指导自组装。在这里，我们描述了由两亲性的α/β-肽与骨架沿α-和β-氨基酸残基1：1交替形成在空气-水界面处形成的单层结构。使用两种α/β肽（一种为双阴离子和另一种为双离子）确定净带负电荷和带正电荷的寡聚物的自组装之间的差异。设计了两个都为两性离子的另外两个α/β肽，以利于在1：1摩尔比的混合物中以相邻链平行取向的方式组装。这些α/β肽在空气-水界面处形成的单分子层的特征在于表面压力-面积等温线，掠入射X射线衍射（GIXD），原子力显微镜和ATR-FTIR。 GIXD数据表明，α/β-肽组装体表现出类似于形成β-折叠的α-肽的衍射特征。衍射数据允许构造具有独特的褶状结构的反平行α/β-肽片的详细模型。一种α/β肽装配体显示出高稳定性，这在以前研究过的α肽装配体中是无与伦比的。 ATR-FTIR数据表明，以平行排列方式组装的两性离子α/β肽的1：1混合物类似于由α肽形成的典型的平行β折叠二级结构。这项研究为两亲性α/β肽的设计建立了指南，该两亲性α/β肽以可预测的方式在空气-水界面处组装，并通过操纵沿骨架的库仑相互作用来控制链间取向。

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