Specific UV photodissociation of tyrosyl-containing peptides in multistage mass spectrometry
Specific UV photodissociation of tyrosyl-containing peptides in multistage mass spectrometry
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DOI：
10.1002/jms.1222
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发表时间：
2007-06-01
影响因子：
2.3
通讯作者：
Lemoine, Jerome
中科院分区：
文献类型：
--
作者：
Joly, Laure;Antoine, Rodolphe;Lemoine, Jerome
在262 nm的紫外光解离（UVPD）已进行了质子化酪氨酰的肽形成的胰蛋白酶消化脱铁转铁蛋白。在UVPD下，主要事件是酪氨酰残基的C-alpha-C-beta键断裂，导致比前体离子低107 Da的自由基离子。这种特异性裂解的解离速率似乎强烈依赖于肽序列，并且在单质子化物种上比在双质子化状态上更突出。由质子化的偶电子天然肽和由UVPD制备的奇电子自由基物种的碰撞活化产生的碎片光谱主要由y-型骨架裂解。它们各自的y-离子模式的比较显示互补性，因为两者的组合增加了肽序列的序列覆盖度。从肽的中性损失的107 Da的具体检测见证了至少一个酪氨酰残基的内容，虽然初步的，提出作为一个潜在的新的过滤策略，在蛋白质数据库搜索。版权所有（c）2007约翰威利父子有限公司。
UV photodissociation (UVPD) at 262 nm has been carried out on protonated tyrosyl-containing peptides formed by trypsin digestion of apo-transferrin. Under UVPD, the main event is the fragmentation of the C-alpha-C-beta bond of the tyrosyl residues leading to a radical ion 107 Da below the precursor ion. The dissociation rate of this specific cleavage appears to be strongly dependent on the peptide sequence and is more prominent on the singly protonated species than on the doubly protonated state. The fragmentation spectra resulting from collisional activation of the protonated even-electron native peptides and of the odd-electron radical species prepared by UVPD are dominated by y-type backbone cleavages. A comparison of their respective y-ion pattern shows complementarities since the combination of both increases the sequence coverage of the peptide sequence. The specific detection of the neutral loss of 107 Da from peptides witnesses the content of at least one tyrosyl residue and, though preliminary, is proposed as a potential new filtering strategy during protein database searching. Copyright (c) 2007 John Wiley & Sons, Ltd.