Study of the fragmentation patterns of the phosphate-arginine noncovalent bond
Study of the fragmentation patterns of the phosphate-arginine noncovalent bond
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DOI：
10.1021/pr050261d
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发表时间：
2005-11-01
影响因子：
4.4
通讯作者：
Woods, AS
中科院分区：
文献类型：
--
作者：
Jackson, SN;Wang, HYJ;Woods, AS
我们以前的工作强调了某些氨基酸残基在多肽之间形成非共价复合体(NCX)中的作用，这些残基主要是一个肽上的两个或两个以上相邻的精氨酸，以及另一个肽上的两个或多个相邻的谷氨酸或天冬氨酸，或者另一个氨基酸上的磷酸化残基。在本研究中，我们利用ESI-MS研究了多巴胺D-2受体第三细胞内环的碱性多肽VLRRRRRKRVN与大麻素CB1羧基末端的磷肽SVSTDpTpSAE的NCX的气相稳定性和解离途径。对VLRRRRRKRVN和SVSTDpTpSAE之间NCX的ESI-MS/MS分析表明，NCX有两条解离途径。主要途径是破坏Arg残基和磷酸基团之间的静电相互作用，同时也记录了另一种途径，即络合物沿着来自Thr或Ser的氧与HPO3之间的共价键解离。为了验证这一替代途径，我们使用离子捕捉仪对两条解离途径的产物离子进行了MS3分析。
Our previous work has highlighted the role of certain amino acid residues, mainly two or more adjacent arginine on one peptide and two or more adjacent glutamate, or aspartate, or a phosphorylated residue on the other in the formation of noncovalent complexes (NCX) between peptides. In the present study, we employ ESI-MS to investigate the gas-phase stability and dissociation pathways of the NCX of a basic peptide VLRRRRKRVN, an epitope from the third intracellular loop of the dopamine D-2 receptor, with the phosphopetide SVSTDpTpSAE, an epitope from the cannabinoid CB1 carboxyl terminus. ESI-MS/MS analysis of the NCX between VLRRRRKRVN and SVSTDpTpSAE suggests two dissociation pathways for the NCX. The major pathway is the disruption of the electrostatic interactions between the Arg residues and the phosphate groups, while an alternative pathway is also recorded, in which the complex is dissociated along the covalent bond between the oxygen from either Thr or Ser and HPO3. To verify the alternative pathway, we have used an ion trap instrument to conduct MS3 analysis on the product ions of both dissociation pathways.