Electron capture dissociation mass spectrometry of phosphopeptides: Arginine and phosphoserine
Electron capture dissociation mass spectrometry of phosphopeptides: Arginine and phosphoserine
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DOI：
10.1016/j.ijms.2015.07.024
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发表时间：
2015-11-15
影响因子：
1.8
通讯作者：
Cooper, Helen J.
中科院分区：
文献类型：
--
作者：
Lopez-Clavijo, Andrea F.;Duque-Daza, Carlos A.;Cooper, Helen J.
我们以前已经表明，磷酸化的存在下，可以抑制检测的电子捕获解离（ECD）片段的双电荷肽离子。盐桥或离子氢键形式的非共价相互作用的存在防止了骨架裂解后片段的分离。在这里，我们显示了一套模型肽的电子捕获解离质谱，旨在研究磷酸丝氨酸和精氨酸位置之间的关系，即AApSA（n）RA（m）KA（n = 0-6，m = 6-0），赖氨酸残基（AApSAAKARAKA）和AAApSARAAAAKAAAK的存在，以及脯氨酸A（A/P）ApSARAAA（A/P）KAAAK的存在。后者类似于先前研究的肽。结果表明，磷酸丝氨酸和碱性氨基酸残基的单独存在不抑制ECD片段化，即使当碱性氨基酸残基的数量大于前体电荷状态。肽序列中脯氨酸的存在也不抑制ECD骨架裂解。然而，磷酸化残基的存在和相对位置确实改变了观察到的骨架片段化丰度。此外，磷酸化的存在似乎抑制精氨酸侧链内的切割，而不管精氨酸残基的相对位置如何。结果表明，ECD片段化行为取决于肽的三维结构，而不是其序列。(C)2015作者由爱思唯尔公司出版
We have previously shown that the presence of phosphorylation can inhibit detection of electron capture dissociation (ECD) fragments of doubly charged peptide ions. The presence of non-covalent interactions, in the form of salt-bridges or ionic hydrogen bonds, prevents the separation of fragments following backbone cleavage. Here, we show the electron capture dissociation mass spectrometry of a suite of model peptides designed to investigate the relationship between phosphoserine and arginine position, namely AApSA(n)RA(m)KA (n = 0-6, m = 6-0), the presence of lysine residues (AApSAAKAARAKA) and AAApSARAAAAKAAAK, and the presence of proline A(A/P)ApSARAAA(A/P)KAAAK. The latter are analogous to the peptides studied previously. The results show that the presence of phosphoserine and basic amino acid residues alone does not inhibit ECD fragmentation, even when the number of basic amino acid residues is greater than the precursor charge state. Neither did the presence of proline in the peptide sequence suppress ECD backbone cleavage. Nevertheless, the presence and relative position of the phosphorylated residue do alter the observed backbone fragmentation abundance. In addition, the presence of phosphorylation appears to inhibit cleavage within the arginine side-chain regardless of the relative position of the arginine residue. The results suggest that ECD fragmentation behaviour is dependent on the three-dimensional structure of a peptide rather than its sequence. (C) 2015 The Authors. Published by Elsevier B.V.