文献类型： 外文期刊

作者： Liu, Ji-hong ¹ ; Cao, Shu-xia ¹ ; Zeng, Zhi-ping ³ ; Liao, Xin-cheng ¹ ; Lu, Jian-sha ¹ ; Zhao, Yu-fen ¹ ;

作者机构： 1.Zhengzhou Univ, Dept Chem, Key Lab Chem Biol & Organ Chem, Zhengzhou 450052, Peoples R China

2.Henan Acad Agr Sci, Res Ctr Agr Qual Stand & Testing Tech, Zhengzhou, Peoples R China

3.Xiamen Univ, Dept Chem, Key Lab Chem Biol Fujian Prov, Xiamen 361005, Peoples R China

4.Xiamen Univ, Coll Chem & Chem Engn, Xiamen, Peoples R China

5.Tsinghua Univ, Dept Chem, Minist Educ, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Beijing 100084, Peoples R China

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 ）

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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.