化学
蛋白质组学
蛋白酵素
自下而上蛋白质组学
串联质谱法
定量蛋白质组学
蛋白酶
无标记量化
串联质量标签
肽
蛋白质组
生物化学
色谱法
质谱法
计算生物学
蛋白质质谱法
酶
生物
基因
作者
T. Mamie Lih,Liyuan Jiao,Lijun Chen,Jongmin Jacob Woo,Yuefan Wang,Hui Zhang
标识
DOI:10.1021/acs.analchem.5c00886
摘要
Liquid chromatography (LC) tandem mass spectrometry (MS/MS) is one of the widely used proteomic techniques to study the alterations occurring at the protein level as well as post-translational modifications (PTMs) of proteins that are relevant to different physiological or pathological statuses. The mass spectrometric analysis of peptides digested from proteins (bottom-up proteomics) has emerged as one of the major approaches for proteomics. In this approach, proteins are first cleaved by one or more proteases into peptides for MS analysis, and peptides with PTMs are further enriched, followed by the LC-MS/MS analysis. To achieve a reproducible and quantitative proteomic characterization, a well-established protease digestion and PTM peptide enrichment protocol is critical. In this study, we developed AUTO-SP, a sample preparation platform providing automated protocols for BCA analysis, protein digestion, and PTM enrichment for protein and PTM analyses. We utilized patient-derived xenograft (PDX) breast cancer tumor tissues (basal-like and luminal subtypes) to demonstrate the efficacy of AUTO-SP. The protein amount was quantified, and proteins were further digested by using AUTO-SP for each PDX sample. Based on the data-independent acquisition (DIA)-MS data, we observed that samples of the same breast cancer subtypes were highly correlated (≥0.98). Additionally, >25,000 phosphopeptides and >14,000 ubiquitinated peptides were identified in the PDX samples when using AUTO-SP for PTM enrichment, while unique pathways were enriched from the differentially expressed ubiquitinated peptides of basal-like and luminal subtypes. AUTO-SP demonstrated its efficacy to provide a reliable and reproducible sample preparation procedure for MS-based proteomic and PTM analyses.
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