The investigation of interaction competition between ATP and DIPP-Ala, Boc-Ala, or Ala by ESI-MS/MS and Theoretical Calculation

文献类型: 外文期刊

第一作者: Liu, Ji-hong

作者: Liu, Ji-hong;Cao, Shu-xia;Liao, Xin-cheng;Lu, Jian-sha;Zhao, Yu-fen;Liu, Ji-hong;Zeng, Zhi-ping;Zhao, Yu-fen;Zeng, Zhi-ping;Zhao, Yu-fen;Zhao, Yu-fen

作者机构:

关键词: ATP;ESI-MS/MS;mini-model of protein;molecular dynamic simulation

期刊名称:PHOSPHORUS SULFUR AND SILICON AND THE RELATED ELEMENTS ( 影响因子:1.082; 五年影响因子:0.859 )

ISSN:

年卷期:

页码:

收录情况: SCI

摘要: The interactions between ATP and N-(O,O-diisopropyl) phosphoryl-L-alanine (DIPP-Ala), N-(tert-butoxycarbonyl)-L-alanine (Boc-Ala), or L-alanine (Ala) were investigated by electrospray ionization tandem mass spectrometry (ESI-MS/MS). The non-covalent complexes between ATP and Boc-Ala or DIPP-Ala were observed, while the complex between ATP and Ala was not found in the mass spectra. The affinity of DIPP-Ala for ATP was confirmed to be stronger than that of Boc-Ala by competition experiment. Through molecular modeling calculations, it was found that the non-covalent complexes were stabilized by intermolecular hydrogen bonds, and the affinity sequence for ATP was DIPP-Ala Boc-Ala Ala by comparing their binding energy, -35.407 kcal/mol, -15.634 kcal/mol, -6.555 kcal/mol, respectively. The results implied that a phosphoryl group was a very important functional group to provide an interaction site between amino acids and ATP, and that N-phosphoryl amino acids can be used as a good model of protein in the studies of molecular recognition of ATP.

分类号: O613

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