Assessing the matrix effects on MALDI-MS in the positive and negative ion mode detection for protein-protected metal nanoclusters

IF 16.4 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Hao Yuan , Djibril Lima , Clothilde Comby-Zerbino , Charlène Bouanchaud , Fabien Chirot , Dipankar Bain , Sanjun Zhang , Rodolphe Antoine
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引用次数: 0

Abstract

Protein-protected metal nanoclusters (MNCs) represent a new class of highly photoluminescent nanomaterials that have wide applications. Suitable reaction conditions combining protein and metal precursors can produce a vast range of different NC sizes (i.e. different number of metal atoms). The average number of metal atoms per protein can be determined by mass spectrometry (MS). MS coupled with matrix-assisted laser desorption ionization (MALDI) presents a number of advantages such as detection with high sensitivity of nanoclusters with high molecular weights. Although many protein-protected MNCs have been characterized by MALDI-MS, a large dispersion in the number of metal atoms has been reported mainly due to sample preparation. In this work, we optimized the protocols for negative and positive ion detection mode as a general MALDI-MS sample preparation method for protein-protected MNCs (bovine serum albumin and lysozyme and with gold and silver). Negative and positive ion mode detection was compared, showing that negative ion mode detection in MALDI-MS can also be used with acidic matrices. Obvious matrix effects on ion signals and peak positions by MALDI-MS were observed. The average metal numbers of MNCs embedded in proteins are different depending on the MALDI matrix. The matrix effects give a warning for more serious consideration on MALDI-MS measurement and spectra analysis of MNCs.

Abstract Image

评估基质对 MALDI-MS 正负离子模式检测蛋白质保护金属纳米团簇的影响
受蛋白质保护的金属纳米团簇(MNCs)是一类新的高光致发光纳米材料,具有广泛的应用前景。在合适的反应条件下,结合蛋白质和金属前体,可以产生多种不同尺寸的 NC(即不同数量的金属原子)。每个蛋白质中金属原子的平均数量可通过质谱法(MS)确定。质谱与基质辅助激光解吸电离(MALDI)联用具有许多优势,例如可以高灵敏度地检测高分子量的纳米团簇。虽然许多受蛋白质保护的 MNCs 已通过 MALDI-MS 鉴定,但有报道称主要由于样品制备的原因,金属原子的数量存在较大的分散性。在这项工作中,我们优化了负离子和正离子检测模式的方案,将其作为蛋白质保护的 MNCs(牛血清白蛋白和溶菌酶以及金和银)的一般 MALDI-MS 样品制备方法。对负离子和正离子检测模式进行了比较,结果表明 MALDI-MS 的负离子检测模式也可用于酸性基质。观察到基质对 MALDI-MS 的离子信号和峰位有明显影响。嵌入蛋白质中的 MNCs 的平均金属数因 MALDI 基质而异。基质效应提醒我们要更认真地考虑 MALDI-MS 测量和 MNCs 图谱分析。
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来源期刊
Accounts of Chemical Research
Accounts of Chemical Research 化学-化学综合
CiteScore
31.40
自引率
1.10%
发文量
312
审稿时长
2 months
期刊介绍: Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.
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