Pathway Selection in Peptide Amphiphile Assembly
Pathway Selection in Peptide Amphiphile Assembly
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DOI：
10.1021/ja503882s
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发表时间：
2014-06-18
影响因子：
15
通讯作者：
Stupp, Samuel I.
中科院分区：
文献类型：
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作者：
Korevaar, Peter A.;Newcomb, Christina J.;Stupp, Samuel I.
超分子结构的性质可能受到其形成过程中所遵循的途径的强烈影响，正如化学反应中的机制和最终结果随所选条件而变化一样。到目前为止，这是一个很大程度上未开发的超分子化学领域。我们在这里演示了如何在水中自组装肽两亲物的不同制备方案可以导致形成不同的超分子形态，无论是含有β-片的长丝或含有无规卷曲构象的肽段的较小聚集体。我们发现，组装成β-片的速度下降，在存在不稳定的“好”溶剂，如六氟异丙醇（HFIP），并在溶液中的瞬态条件的影响。此外，肽两亲物研究自发成核的β-折叠含丝在HFIP在水中的临界分数低于21%。此外，片材组件具有高的动力学稳定性，并且一旦形成，就不会迅速分解。我们预见，洞察到的超分子系统的特征动力学提供了一种有效的方法来选择必要的功能的最佳组装途径。
The nature of supramolecular structures could be strongly affected by the pathways followed during their formation just as mechanisms and final outcomes in chemical reactions vary with the conditions selected. So far this is a largely unexplored area of supramolecular chemistry. We demonstrate here how different preparation protocols to self-assemble peptide amphiphiles in water can result in the formation of different supramolecular morphologies, either long filaments containing beta-sheets or smaller aggregrates containing peptide segments in random coil conformation. We found that the assembly rate into beta-sheets decreases in the presence of a destabilizing "good" solvent like hexafluoroisopropanol (HFIP) and is affected by transient conditions in solution. Also the peptide amphiphile investigated spontaneously nucleates the beta-sheet-containing filaments at a critical fraction of HFIP in water below 21%. Furthermore, sheet assemblies have a high kinetic stability and, once formed, do not disassemble rapidly. We foresee that insights into the characteristic dynamics of a supramolecular system provide an efficient approach to select the optimum assembly pathway necessary for function.