基质辅助激光解吸/电离源内衰减质谱分析多肽和蛋白质的机理研究进展:电子转移反应是碎片化的起始步骤。

IF 6.6 2区 化学 Q1 SPECTROSCOPY
Daiki Asakawa
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引用次数: 0

摘要

由于基质辅助激光解吸/电离源内衰变(MALDI-ISD)诱导多肽主链上的选择性切割,该技术可以可靠地鉴定多肽和蛋白质。在过去的15年里,一些新的基质被开发出来,更有效地诱导MALDI-ISD,开辟了新的研究途径。MALDI-ISD对多肽的断裂可分为两类:还原基质和氧化基质分别诱导N-Cα和c - α- c键的选择性断裂。关于解离机制,MALDI-ISD直到最近才被认为是由分析物肽和基质之间的“氢原子”转移引起的。基于这一假设,氢原子的来源可能是MALDI中还原基质的苯胺基和MALDI- isd中氧化基质的肽主链的酰胺氮。MALDI-ISD参与了N-H键的均裂,尽管N-H键通常比O-H和C-H键更强。值得注意的是,质谱实验无法区分“氢原子转移”和“电子转移和随后的质子转移”。最近精心设计的实验和量子化学计算强烈表明,肽和基质之间的电子转移可能是MALDI-ISD过程的第一步。MALDI-ISD的还原和氧化基质分别通过肽自由基阴离子和阳离子诱导断裂。产生的碎片离子和自由基随后在MALDI羽流中发生反应,导致在质谱中可检测到的稳定的偶数电子离子的形成。因此,MALDI-ISD片段被观察为带正电荷和负电荷的离子,尽管MALDI-ISD会导致肽自由基阴离子和阳离子的分裂。提出的机制为理解MALDI-ISD过程提供了一个健壮的框架。更全面地了解这一过程对于充分利用MALDI-ISD技术的潜力至关重要,并将为进一步发展以寻找新矩阵为基础的分析化学领域的方法铺平道路。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Advances in the Mechanistic Understanding of Matrix-Assisted Laser Desorption/Ionization In-Source Decay Mass Spectrometry for Peptides and Proteins: Electron Transfer Reaction as the Initiating Step of Fragmentation.

Because matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) induces selective cleavage on the peptide backbone, this technique allows reliable identification of peptides and proteins. In the last 15 years, several new matrices have been developed that more efficiently induce MALDI-ISD, opening new research avenues. Fragmentation of peptides by MALDI-ISD can be divided into two categories: reducing and oxidizing matrices induce selective cleavage of N-Cα and Cα-C bonds, respectively. Regarding the dissociation mechanism, MALDI-ISD was believed, until recently, to be initiated by "hydrogen atom" transfer between an analyte peptide and the matrix. Based on this hypothesis, the origin of the hydrogen atoms would be the aniline group of the matrix in MALDI with a reducing matrix and the amide nitrogen of the peptide backbone in MALDI-ISD with an oxidizing matrix. MALDI-ISD involves homolytic cleavage of N-H bonds, though the N-H bond is generally stronger than O-H and C-H bonds. Notably, mass spectrometry experiments cannot distinguish between "hydrogen atom transfer" and "electron transfer and subsequent proton transfer." Recent well-designed experiments and quantum chemistry calculations have strongly suggested that electron transfer between the peptide and matrix is likely to be the initial step of the MALDI-ISD process. Reducing and oxidizing matrices for MALDI-ISD induce fragmentation through peptide radical anions and cations, respectively. The generated fragment ions and radicals subsequently undergo reactions within the MALDI plume, leading to the formation of stable even-electron ions that are detectable in the mass spectrum. As a result, MALDI-ISD fragments are observed as both positively and negatively charged ions, despite MALDI-ISD entailing the fragmentation of peptide radical anions and cations. The proposed mechanism offers a robust framework for understanding the MALDI-ISD process. A more comprehensive understanding of this process is essential to fully harness the potential of the MALDI-ISD technique and would pave the way for further development of methodologies advancing the field of analytical chemistry based on finding new matrices.

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来源期刊
Mass Spectrometry Reviews
Mass Spectrometry Reviews 物理-光谱学
CiteScore
16.30
自引率
3.00%
发文量
56
期刊介绍: The aim of the journal Mass Spectrometry Reviews is to publish well-written reviews in selected topics in the various sub-fields of mass spectrometry as a means to summarize the research that has been performed in that area, to focus attention of other researchers, to critically review the published material, and to stimulate further research in that area. The scope of the published reviews include, but are not limited to topics, such as theoretical treatments, instrumental design, ionization methods, analyzers, detectors, application to the qualitative and quantitative analysis of various compounds or elements, basic ion chemistry and structure studies, ion energetic studies, and studies on biomolecules, polymers, etc.
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