Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer.
Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer.
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DOI：
10.1016/j.ijms.2014.04.015
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发表时间：
2014-06-15
影响因子：
1.8
通讯作者：
Eyers CE
中科院分区：
文献类型：
--
作者：
Gonzalez-Sanchez MB;Lanucara F;Hardman GE;Eyers CE
在QIT中通过CID评估含氨基磷酸酯的肽的片段化。pHis同二聚体的形成促进CID期间的分子间磷酸盐转移。二聚体的形成和磷酸转移依赖于C-末端的碱性赖氨酸。在低能碰撞诱导解离（CID）中，碱性残基的质子化侧链与磷酸肽的带负电荷的磷酸基之间形成的氢键和静电相互作用在控制它们的解离途径中起着至关重要的作用。了解氨基磷酸酯（即磷酸组氨酸，磷赖氨酸和磷酸精氨酸），而不是含磷酸单酯的肽在CID过程中的行为是至关重要的，在调查这些有问题的物种串联质谱。为此，通过使用Paul型离子阱（Amazon，Bruker）的ESI-MS和通过行波离子迁移率-质谱法（Synapt G2-Si，沃茨）分析含有磷酸组氨酸（pHis）或磷赖氨酸（pLys）的合成肽。低能量CID的产品的分析表明，形成了一个双重的“磷酸化”的产品离子所产生的分子间气相磷酸转移内的磷酸肽二聚体。结果解释了形成的同型二聚体磷酸组氨酸（pHis）肽非共价复合物（NCX），可能稳定的pHis磷酸基团和质子化的C-末端赖氨酸残基的肽之间的静电相互作用。据我们所知，这是第一次报告的分子间气相磷酸转移从一个磷酸肽到另一个，导致一个双重磷酸化的肽产品离子。
Fragmentation of phosphoramidate-containing peptides by CID in a QIT was assessed. pHis homodimer formation facilitates intermolecular phosphate transfer during CID. Dimer formation and phosphate transfer is dependent on a C-terminal basic Lys. The hydrogen bonds and electrostatic interactions that form between the protonated side chain of a basic residue and the negatively charged phosphate of a phosphopeptide can play crucial roles in governing their dissociation pathways under low-energy collision-induced dissociation (CID). Understanding how phosphoramidate (i.e. phosphohistidine, phospholysine and phosphoarginine), rather than phosphomonoester-containing peptides behave during CID is paramount in investigation of these problematic species by tandem mass spectrometry. To this end, a synthetic peptide containing either phosphohistidine (pHis) or phospholysine (pLys) was analyzed by ESI-MS using a Paul-type ion trap (AmaZon, Bruker) and by traveling wave ion mobility-mass spectrometry (Synapt G2-Si, Waters). Analysis of the products of low-energy CID demonstrated formation of a doubly ‘phosphorylated’ product ion arising from intermolecular gas-phase phosphate transfer within a phosphopeptide dimer. The results are explained by the formation of a homodimeric phosphohistidine (pHis) peptide non-covalent complex (NCX), likely stabilized by the electrostatic interaction between the pHis phosphate group and the protonated C-terminal lysine residue of the peptide. To the best of our knowledge this is the first report of intermolecular gas-phase phosphate transfer from one phosphopeptide to another, leading to a doubly phosphorylated peptide product ion.
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影响因子：
8
作者：
Medzihradszky, KF;Phillipps, NJ;Turck, CW
通讯作者：
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影响因子：
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DOI：
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发表时间：
2008-10
影响因子：
3.2
作者：
Jackson SN;Moyer SC;Woods AS
通讯作者：
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