Quantitative analysis of low-abundance serological proteins with peptide affinity-based enrichment and pseudo-multiple reaction monitoring by hybrid quadrupole time-of-flight mass spectrometry

被引:14
|
作者
Kim, Kwang Hoe [1 ,3 ]
Ahn, Yeong Hee [2 ]
Ji, Eun Sun [1 ]
Lee, Ju Yeon [1 ]
Kim, Jin Young [1 ]
An, Hyun Joo [3 ]
Yoo, Jong Shin [1 ,3 ]
机构
[1] Korea Basic Sci Inst, Div Mass Spectrometry, Ochang 363883, Cheongju Chungb, South Korea
[2] Cheongju Univ, Dept Biomed Sci, Cheongju 363764, South Korea
[3] Chungnam Natl Univ, Grad Sch Analyt Sci & Technol, Taejon 305764, South Korea
关键词
Low-abundance serological protein; Peptide affinity-based enrichment; Pseudo-multiple reaction monitoring; Hybrid quadrupole time-of-flight mass spectrometer; LINEAR ION-TRAP; N-ACETYLGLUCOSAMINYLTRANSFERASE-V; TISSUE INHIBITOR; COLON-CANCER; TARGETED PROTEOMICS; COLORECTAL-CANCER; DRUG METABOLITES; PLASMA; SERUM; METALLOPROTEINASE-1;
D O I
10.1016/j.aca.2015.04.033
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Multiple reaction monitoring (MRM) is commonly used for the quantitative analysis of proteins during mass pectrometry (MS), and has excellent specificity and sensitivity for an analyte in a complex sample. In this study, a pseudo-MRM method for the quantitative analysis of low-abundance serological proteins was developed using hybrid quadrupole time-of-flight (hybrid Q-TOF) MS and peptide affinity-based enrichment. First, a pseudo-MRM-based analysis using hybrid Q-TOF MS was performed for synthetic peptides selected as targets and spiked into tryptic digests of human serum. By integrating multiple transition signals corresponding to fragment ions in the full scan MS/MS spectrum of a precursor ion of the target peptide, a pseudo-MRM MS analysis of the target peptide showed an increased signal-to-noise (S/N) ratio and sensitivity, as well as an improved reproducibility. The pseudo-MRM method was then used for the quantitative analysis of the tryptic peptides of two low-abundance serological proteins, tissue inhibitor of metalloproteinase 1 (TIMP1) and tissue-type protein tyrosine phosphatase kappa (PTP kappa), which were prepared with peptide affinity-based enrichment from human serum. Finally, this method was used to detect femtomolar amounts of target peptides derived from TIMP1 and PTPk, with good coefficients of variation (CV 2.7% and 9.8%, respectively), using a few microliters of human serum from colorectal cancer patients. The results suggest that pseudo-MRM using hybrid Q-TOF MS, combined with peptide affinity-based enrichment, could become a promising alternative for the quantitative analysis of low-abundance target proteins of interest in complex serum samples that avoids protein depletion. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:38 / 48
页数:11
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