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首页> 外文期刊>Journal of mass spectrometry: JMS >The role of basic residues in the fragmentation process of the lysine rich cell-penetrating peptide TP10
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The role of basic residues in the fragmentation process of the lysine rich cell-penetrating peptide TP10

机译：碱性残基在富含赖氨酸的细胞穿透肽TP10片段化过程中的作用

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摘要

Selective cleavage effect of basic residues in the fragmentation of short peptides has been studied intensively. In contrast, the role of basic residues in the degradation of large peptides, such as cell-penetrating peptides, is largely unknown. In this work, the fragmentation of a 21 residues cell-penetrating peptide TP10 containing four lysine residues was studied by collision-induced dissociation mass spectrometry and computation methods. The influence of lysine residues on amide bond cleavage and fragmentation products was investigated. The results revealed that the selective cleavage effect of lysine residue did not present when the adjacent lysine residues in TP10 were both protonated. The localized high positive charge density might be the reason of preventing the mobile proton from migrating to the amide bonds in this part of the peptide. In contrast, the mobile proton preferred to reside in the N-terminal part of TP10 which had less positive charge. This preference gave more information of the peptide sequence in the mass spectrometry study and was helpful for stabilizing the C-terminal part of TP10, in which the basic lysine residues were preserved and crucial to the cell-penetrating process. Copyright (c) 2015 John Wiley & Sons, Ltd.
机译：深入研究了碱性残基在短肽片段化中的选择性切割作用。相比之下，基本残基在诸如细胞穿透肽之类的大肽降解中的作用是未知的。在这项工作中，通过碰撞诱导解离质谱法和计算方法研究了21个残基的穿透细胞的肽TP10的片段，该肽含有四个赖氨酸残基。研究了赖氨酸残基对酰胺键裂解和片段化产物的影响。结果表明，当TP10中相邻的赖氨酸残基均被质子化时，不存在赖氨酸残基的选择性裂解作用。局部高正电荷密度可能是阻止移动质子迁移到该部分肽中酰胺键的原因。相反，可移动质子优选驻留在TP10的N端部分，该部分的正电荷较少。这种偏好在质谱研究中提供了有关肽序列的更多信息，并有助于稳定TP10的C端部分，其中保留了赖氨酸的基本残基，并且对细胞穿透过程至关重要。版权所有（c）2015 John Wiley＆Sons，Ltd.

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