Programming the internal structure and stability of helical pores self-assembled from dendritic dipeptides via the protective groups of the peptide
Programming the internal structure and stability of helical pores self-assembled from dendritic dipeptides via the protective groups of the peptide
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DOI：
10.1021/ja056313h
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发表时间：
2005-12-21
影响因子：
15
通讯作者：
Heiney, PA
中科院分区：
文献类型：
--
作者：
Percec, V;Dulcey, AE;Heiney, PA
报道了树枝状二肽（4- 3，4 - 3，5）12 G2-CH 2-X-L-Tyr-L-Ala-OMe（X = Boc，Moc，Ac）的合成，在本体和溶液中的自组装，及其超分子螺旋多孔组装体的结构和逆结构分析。的尺寸，结构，内部秩序，超分子螺旋孔的热稳定性，和构象的树枝状和超分子树枝状大分子的编程由clipeparticle的保护基团的性质。保护基团对螺旋孔的结构进行编程的能力揭示了最简单的设计策略，其补充了基于树枝化基元的架构、立体化学和二肽的结构的更复杂的策略。
The synthesis of dendritic dipeptides (4-3,4-3,5)12G2-CH2-X-L-Tyr-L-Ala-OMe with X = Boc, Moc, and Ac; their self-assembly in bulk and in solution; and the structural and retrostructural analysis of their supramolecular helical porous assemblies are reported. The dimensions, structure, internal order, thermal stability of the supramolecular helical pores, and conformations of the dendron and supramolecular dendrimer are programmed by the nature of the protective groups of the clipepticle. The ability of the protective groups to program the structure of the helical pore reveals the simplest design strategy that complements the more complex strategies based on the architecture of the dendron, the stereochemistry, and the structure of the dipeptide.