Collagen fibers as a chiral agent: A demonstration of stereochemistry effects.
Collagen fibers as a chiral agent: A demonstration of stereochemistry effects.
复制标题
胶原纤维作为手性剂：立体化学效应的演示。
DOI：
10.1021/ja065047k
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发表时间：
2006
影响因子：
15
通讯作者：
G. Navon
中科院分区：
文献类型：
--
作者：
U. Eliav;G. Navon
胶原蛋白是人体内最常见的蛋白质。因此，它与小分子，特别是氨基酸的相互作用令人感兴趣。由于肌腱中胶原纤维的高度有序性，与其相互作用的小分子的1H-1H和1H-13 C偶极相互作用以及2 H四极相互作用的平均值不为零。在目前的工作中，我们报告说，这些残留的相互作用丙氨酸在完整的肌腱是显着不同的l和d的对映体，这意味着胶原蛋白在其天然状态作为一个手性剂。不同的l/d比率为每一个残留的相互作用沿着不同的载体在丙氨酸分子和类似的转移NOE从胶原蛋白的l和d对映异构体表明，不同的残留的偶极和四极相互作用的主要来源是立体化学的结合，而不是结合的分子的量。
The collagen is the most common protein in mammalians. Thus its interaction with small molecules and particularly amino acids is of interest. Owing to the high degree of order of collagen fibers in a tendon, the 1H-1H and 1H-13C dipolar interactions and the 2H quadrupolar interaction of small molecules interacting with it do not average to zero. In the present work we report that these residual interactions for alanine in intact tendons are significantly different for the l and d enantiomers meaning that the collagen in its native state acts as a chiral agent. The different l/d ratios for each of the residual interactions along the different vectors in the alanine molecule and the similarly transferred NOE from the collagen to the l and d enantiomers indicate that the main source of the different residual dipolar and quadrupolar interactions is the stereochemistry of the binding and not the amounts of bound molecules.