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首页> 外文期刊>Macromolecules >Self-assembling peptide-polymer conjugates comprising D-alt-L)-cyclopeptides as aggregator domains
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Self-assembling peptide-polymer conjugates comprising D-alt-L)-cyclopeptides as aggregator domains

机译：包含D-alt-L）-环肽作为聚集域的自组装肽-聚合物共轭物

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摘要

The synthesis of peptide-polymer conjugates comprising (D-alt-L)-cyclopeptides as aggregator domains and their self-assembly into tubelike structures is described. By coupling two well-defined poly(n-butyl acrylate) blocks to opposite sides of a preformed cyclic (D-alt-L)-alpha-octapeptide, a coil-ring-coil bioconjugate was accessed. The applied solution-phase coupling route allowed a multigram scale synthesis of the conjugate and assured both a controlled synthesis and ease of analysis. The controlled self-assembly of the conjugate leads to uniform tube structures. Atomic force microscopy (AFM) of these aggregates deposited on mica revealed a height of 1.4 +/- 0.2 nm, a width of 5 nm, and roughly estimated lengths of up to 200-300 nm. A model is proposed, explaining the structure dimensions. This includes the formation of a tubular peptide core build via stacking of the cyclopeptides and a poly(n-butyl acrylate) shell wrapping around the peptide tube. The model is consistent with infrared spectroscopy and electron diffraction measurements, verifying that the peptide segment of the conjugate adopts a beta-sheet structure, similar to unsubstituted (D-alt-L)-cyclopeptides. Hence, the stacks of peptide rings are stabilized along the fiber axis via inter-ring beta-sheet H-bonding. The tube structures are capable to interact laterally, organizing further into weak networks as was evidenced by AFM and transmission electron microscopy.
机译：描述了包含（D-alt-L）-环肽作为聚集域的肽-聚合物缀合物的合成及其自组装成管状结构的方法。通过将两个定义明确的聚（丙烯酸正丁酯）嵌段偶联到预先形成的环状（D-alt-L）-α-八肽的相对侧，可以得到线圈-环-线圈生物缀合物。所应用的溶液-相偶联途径允许缀合物的克级合成，并确保可控合成和易于分析。结合物的受控自组装导致均匀的管结构。这些沉积在云母上的聚集体的原子力显微镜（AFM）显示高度为1.4 +/- 0.2 nm，宽度为5 nm，粗略估计的长度可达200​​-300 nm。提出了一个模型，解释了结构尺寸。这包括通过堆叠环肽和包裹在肽管周围的聚（丙烯酸正丁酯）壳形成管状肽核心结构。该模型与红外光谱和电子衍射测量结果一致，证实了缀合物的肽段采用了β-折叠结构，类似于未取代的（D-alt-L）-环肽。因此，肽环的堆叠通过环间β-折叠H键沿纤维轴稳定。管结构能够横向相互作用，进一步组织成薄弱的网络，如AFM和透射电子显微镜所证明的。

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