Helical peptoid mimics of lung surfactant protein C.
Helical peptoid mimics of lung surfactant protein C.
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DOI：
10.1016/j.chembiol.2003.10.008
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发表时间：
2003-11
影响因子：
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通讯作者：
Cindy W. Wu;Shannon L. Seurynck;Ka Yee C. Lee;A. Barron
中科院分区：
文献类型：
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作者：
Cindy W. Wu;Shannon L. Seurynck;Ka Yee C. Lee;A. Barron
在作为新型生物材料和治疗剂开发的拟肽折叠体家族中，具有α-手性侧链的聚-N-取代的甘氨酸（类肽）因其在有机和水溶液中采用稳定的螺旋二级结构的能力而特别令人感兴趣。在这里，我们表明，肽类22聚体与仿生序列的侧链和两亲性，螺旋二级结构作为一个很好的模拟表面活性剂蛋白C（SP-C），一个小的蛋白质，在表面活性剂替代治疗新生儿呼吸窘迫综合征中起着重要的作用。当整合到脂质膜中时，螺旋类肽SP模拟物捕获天然蛋白质的基本表面活性行为。这项工作提供了一个例子，说明密切模拟天然蛋白质的疏水/极性序列模式和折叠的非生物低聚物如何也可以模拟其生物物理功能。
Among the families of peptidomimetic foldamers under development as novel biomaterials and therapeutics, poly-N-substituted glycines (peptoids) with α-chiral side chains are of particular interest for their ability to adopt stable, helical secondary structure in organic and aqueous solution. Here, we show that a peptoid 22-mer with a biomimetic sequence of side chains and an amphipathic, helical secondary structure acts as an excellent mimic of surfactant protein C (SP-C), a small protein that plays an important role in surfactant replacement therapy for the treatment of neonatal respiratory distress syndrome. When integrated into a lipid film, the helical peptoid SP mimic captures the essential surface-active behaviors of the natural protein. This work provides an example of how an abiological oligomer that closely mimics both the hydrophobic/polar sequence patterning and the fold of a natural protein can also mimic its biophysical function.