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首页> 外文期刊>Journal of mass spectrometry: JMS >Heterogeneity of peptide adducts with carbonylated lipid peroxidation products
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Heterogeneity of peptide adducts with carbonylated lipid peroxidation products

机译：肽加合物与羰基化脂质过氧化产物的异质性

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摘要

Highly reactive lipid peroxidation-derived carbonyls (oxoLPP) modify protein nucleophiles via Michael addition or Schiff base formation. Once formed, Michael adducts can be further stabilized via cyclic hemiacetals with or without loss of water. Depending on the mechanism of their formation, peptide-oxoLPP can carry aldehyde or keto groups and thus be a part of the total protein carbonylation level. If a carbonyl function is lost during consecutive reactions, the oxoLPP-peptide adducts will not be detected using the common carbonyl labeling protocols. Because of the differences in adduct stabilities, it is possible to address the heterogeneity of peptide/protein-oxoLPP adducts by careful evaluation of tandem mass spectra of modified peptides. Here, we used hydrophilic interaction liquid chromatography-tandem mass spectrometry analysis of lysine, cysteine and histidine containing model peptides co-incubated with oxidized 1-palmitoyl-2-linoleoyl-sn-glycerophosphatidylcholine to characterize the collision-induced dissociation behavior of peptide-carbonyl adducts. Numerous modifications were detected based on the analysis of tandem mass spectra, including Schiff bases on lysine (two), Michael adducts on lysine (six), cysteine (eleven) and histidine (two), as well as 4-hydroxy-2-aldehydes derived dehydrated cyclic hemiacetals on cysteine (five) and histidine (one). Additionally, cysteine and histidine side chains were modified by lipid-bound aldehydes as Michael adducts and dehydrated hemiacetals. The tandem mass spectra revealed collision-induced dissociation characteristics specific for each class of oxoLPP-peptide adducts. Copyright (c) 2015 John Wiley & Sons, Ltd.
机译：高反应性脂质过氧化衍生的羰基（oxoLPP）通过迈克尔加成或席夫碱形成修饰蛋白质亲核试剂。一旦形成，迈克尔加合物可通过环状半缩醛进一步稳定，而不会失水。根据它们的形成机理，肽-oxoLPP可以带有醛基或酮基，因此是总蛋白质羰基化水平的一部分。如果在连续反应中失去羰基功能，则无法使用常见的羰基标记方案检测到oxoLPP-肽加合物。由于加合物稳定性的差异，可以通过仔细评估修饰肽的串联质谱图来解决肽/蛋白质-oxoLPP加合物的异质性。在这里，我们使用亲水相互作用液相色谱-串联质谱法对含有赖氨酸，半胱氨酸和组氨酸的模型肽与氧化的1-棕榈酰基-2-亚油酰基-sn-甘油磷脂酰胆碱共孵育进行了分析，以表征碰撞引起的肽-羰基解离行为加合物。根据串联质谱分析检测到许多修饰，包括赖氨酸上的席夫碱（两个），赖氨酸上的迈克尔加合物（六个），半胱氨酸（十一个）和组氨酸（两个）以及4-羟基-2-醛衍生的半胱氨酸（五个）和组氨酸（一个）上的脱水环状半缩醛。另外，半胱氨酸和组氨酸侧链被脂质结合的醛修饰为迈克尔加合物和脱水的半缩醛。串联质谱揭示了每类oxoLPP肽加合物特有的碰撞诱导解离特性。版权所有（c）2015 John Wiley＆Sons，Ltd.

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