Conformations of spermine in adenosine triphosphate complex : The structural basis for weak bimolecular interactions of major cellular electrolytes
Conformations of spermine in adenosine triphosphate complex : The structural basis for weak bimolecular interactions of major cellular electrolytes
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三磷酸腺苷复合物中精胺的构象：主要细胞电解质弱双分子相互作用的结构基础
DOI：
10.1002/chem.201002759
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发表时间：
2011
期刊：
影响因子：
--
通讯作者：
et al
中科院分区：
文献类型：
--
作者：
Maruyoshi;K.;et al
合成了选择性2h -和13c -标记的精胺（SPM），并用核磁共振谱分析了6个构象相关键的自旋-自旋耦合常数。由三个烷基基团、一个丁烯和两个丙烯链组成的SPM在与多价阴离子（如三磷酸腺苷（ATP）、ATP - mg2 +和三聚磷酸）相互作用时发生构象变化。在与ATP相互作用后，影响相邻铵基对（即N1/N5和N5/N5 '）之间距离的C - _ - C键，相对于4 HCl盐的SPM，增加了17 - 20%的gaucherotamers的数量。然而，SPM-ATP复合物的高构象物的增量趋势与亚精胺(SPD) -ATP复合物的增量趋势有很大不同。这表明SPM可能优先识别ATP的腺苷基而不是三聚磷酸部分。这可能是SPM对ATP-Mg2 +的亲和力高于SPD的原因，SPD主要与β -和γ -磷酸盐相互作用，很容易被Mg2+取代。这些结果为进一步了解多胺生物功能的结构基础提供了线索。
Selectively2H‐ and13C‐labeled spermines (SPM) were efficiently synthesized and analyzed by NMR spectroscopy to determine the spin–spin coupling constants for six conformationally relevant bonds. SPM that is composed of three alkyl moieties, a butanylene, and two propanylene chains undergoes a conformational change when interacting with multivalent anions (e.g., adenosine triphosphate (ATP), ATP–Mg2+, and tripolyphosphate). Upon interaction with ATP, the CC bonds, which affect the distance between the neighboring pairs of ammonium groups (i.e., N1/N5 and N5/N5′), increase the population ofgaucherotamers by 17–20 % relative to those in the 4 HCl salt of SPM. However, the trend in increments of thegaucheconformers for the SPM–ATP complex profoundly differs from that of the spermidine (SPD)–ATP complex. This implies that SPM may preferentially recognize the adenyl group of ATP rather than the tripolyphosphate moiety. This may account for the higher affinity of SPM to ATP–Mg2+than with that of SPD, which chiefly interacts with β‐ and γ‐phosphates and is easily replaced by Mg2+. These results may provide a clue for the further understanding of the structural basis of polyamine biological functions.