Diversity in Gold Finger Structure Elucidated by Traveling-Wave Ion Mobility Mass Spectrometry
Diversity in Gold Finger Structure Elucidated by Traveling-Wave Ion Mobility Mass Spectrometry
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DOI：
10.1002/anie.201612494
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发表时间：
2017-04-10
影响因子：
16.6
通讯作者：
Farrell, Nicholas P.
中科院分区：
文献类型：
--
作者：
Du, Zhifeng;de Paiva, Raphael E. F.;Farrell, Nicholas P.
行波离子迁移率（TWIM）质谱（MS）是一种用于蛋白质和肽的结构和构象分析的强大方法，能够区分具有相同序列但在不同残基处被修饰的异构肽（或蛋白质）。在这项研究中，TWIM-MS技术被用来分离异构体金金属肽离子形成的Zn-II位移从父锌指（ZF）。合成的金手指肽衍生自HIV核衣壳p7蛋白（NCp 7-F2）的C-末端和Sp1转录因子（Sp1-F3）的手指3。TWIM-MS能够获得不同的产品离子光谱的每一种异构体，清楚地表明在存在多种协调可能性的主要构象的结合位点。碰撞截面测量表明，金化肽具有比母体锌化合物NCp 7-F2稍微更紧凑的结构，其仅显示一种构象。
Traveling wave ion mobility (TWIM) mass spectrometry (MS) is a powerful method for the structural and conformational analysis of proteins and peptides, enabling the differentiation of isomeric peptides (or proteins) that have the same sequence but are modified at different residues. In this study, the TWIM-MS technique was used to separate isomeric AuI metallopeptide ions that were formed by Zn-II displacement from the parent zinc fingers (ZFs). The synthetic gold finger peptides were derived from the C-terminus of the HIV nucleocapsid p7 protein (NCp7-F2) and finger 3 of the Sp1 transcription factor (Sp1-F3). TWIM-MS enabled the acquisition of distinct product ion spectra for each isomer, clearly indicating the binding sites for the major conformers in the presence of multiple coordination possibilities. Collision crosssection measurements showed that the aurated peptide has a slightly more compact structure than the parent zinc compound NCp7-F2, which showed only one conformation.