Investigating Anion Effects on Metal Ion Binding Interactions With Amyloid β Peptide by Ion Mobility Mass Spectrometry

IF 1.9 3区 化学 Q3 BIOCHEMICAL RESEARCH METHODS Journal of Mass Spectrometry Pub Date : 2024-09-27 DOI:10.1002/jms.5090
Jingwei Zhang, Ashley Phetsanthad, Lingjun Li
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Abstract

The study of metal ion's role in the biological processes of Alzheimer's disease has spurred investigations into the coordination chemistry of amyloid beta peptide and its fragments. Nano-electrospray ionization mass spectrometry (nESI-MS) has been utilized to examine the stabilization of bound anions on multiprotein complexes without bulk solvent. However, the effects of anions on metal ion binding interactions with amyloid beta peptide have not been explored. This study directly examined metal-peptide complexes using nESI-MS and investigated the effects of various anions on the binding ratio and stability of these complexes from ammonium salt solutions. The results indicate that different anions have distinct effects on the binding ratio and stability of various metal-peptide complexes. Of these, the bicarbonate ion exhibits the highest binding ratios for metal-peptide complexes, while binding ratios for these complexes in phosphate are comparatively low. Our results suggest that acetate, formate, bicarbonate, and phosphate have weak affinities and act as weak stabilizers of the metal-peptide complex structure in the gas phase. Intriguingly, chloride and sulfate act as stabilizers of the metal-peptide complex in the gas phase. The rank order determined from these data is substantially different from the Hofmeister salt series in solution. Although this outcome was anticipated due to the reduced influence of anions and water solvation, our findings correlate well with expected anion binding in solution and emphasize the importance of both hydration layer and anion-metal-peptide binding effects for Hofmeister-type stabilization in solution. This approach proved useful in examining the interactions between metal ions and amyloid beta peptide, which are relevant to Alzheimer's disease, using direct ESI-MS.

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用离子迁移质谱法研究阴离子对金属离子与淀粉样β肽结合相互作用的影响
对金属离子在阿尔茨海默病生物过程中作用的研究促使人们对淀粉样 beta 肽及其片段的配位化学进行研究。纳米电喷雾离子化质谱(nESI-MS)已被用于研究结合阴离子对无大量溶剂的多蛋白复合物的稳定作用。然而,阴离子对金属离子与淀粉样 beta 肽结合相互作用的影响尚未得到探讨。本研究利用 nESI-MS 直接检测了金属肽复合物,并从铵盐溶液中研究了各种阴离子对这些复合物的结合率和稳定性的影响。结果表明,不同的阴离子对各种金属肽复合物的结合率和稳定性有不同的影响。其中,碳酸氢根离子与金属肽复合物的结合率最高,而这些复合物在磷酸盐中的结合率相对较低。我们的研究结果表明,醋酸盐、甲酸盐、碳酸氢盐和磷酸盐的亲和力较弱,在气相中对金属肽复合物结构起着微弱的稳定作用。耐人寻味的是,氯化物和硫酸盐在气相中起着金属肽复合物稳定剂的作用。根据这些数据确定的等级顺序与溶液中的霍夫迈斯特盐系列有很大不同。尽管由于阴离子和水溶作用的影响减弱,这一结果在意料之中,但我们的研究结果与溶液中阴离子结合的预期结果有很好的相关性,并强调了水合层和阴离子-金属肽结合效应对于溶液中霍夫迈斯特型稳定的重要性。事实证明,这种方法有助于利用直接 ESI-MS 方法研究金属离子与淀粉样 beta 肽之间的相互作用,这与阿尔茨海默氏症有关。
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来源期刊
Journal of Mass Spectrometry
Journal of Mass Spectrometry 化学-光谱学
CiteScore
5.10
自引率
0.00%
发文量
84
审稿时长
1.5 months
期刊介绍: The Journal of Mass Spectrometry publishes papers on a broad range of topics of interest to scientists working in both fundamental and applied areas involving the study of gaseous ions. The aim of JMS is to serve the scientific community with information provided and arranged to help senior investigators to better stay abreast of new discoveries and studies in their own field, to make them aware of events and developments in associated fields, and to provide students and newcomers the basic tools with which to learn fundamental and applied aspects of mass spectrometry.
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