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Zhang W, Chen J, Xie L. Optical biosensor arrays based on nanozymes for environmental monitoring and food safety detection: principles, design, and applications. ANALYTICAL METHODS : ADVANCING METHODS AND APPLICATIONS 2025; 17:882-891. [PMID: 39749857 DOI: 10.1039/d4ay02088j] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Track Full Text] [Subscribe] [Scholar Register] [Indexed: 01/04/2025]
Abstract
Typical biosensing platforms are based on the "lock-and-key" approach, providing high specificity and sensitivity for environmental and food safety monitoring. However, they are limited in their ability to detect multiple analytes simultaneously. With the use of pattern identification methods, biosensor arrays can detect faint fluctuations caused by multiple analytes with similar properties in complex systems. As a simple and efficient detection tool, optical biosensor arrays have become crucial for on-site and visible environmental and food safety monitoring. To enhance their practical applications, enzyme-like nanomaterial (nanozyme)-based biosensor arrays have been developed and integrated into optical biosensing platforms, leveraging their exposed active sites and tunable catalytic capabilities. For the development of an optical biosensor array, it is essential to incorporate multiple biosensing elements that can specifically interact with analytes to produce distinct "fingerprint" signals, enabling the differentiation of different targets via pattern identification. This review provides a comprehensive overview of nanozyme-based optical biosensor arrays for environmental and food safety monitoring. It explores the selective approaches of nanozyme-based colorimetric and fluorescent biosensor arrays, compares detection platforms utilizing nanozyme systems, and emphasizes the application of nanozyme-based optical biosensor arrays for environmental and food hazard monitoring. By evaluating current trends and summarizing both prospects and challenges, this review offers valuable guidance for the rational design of unique nanozyme-based optical biosensor arrays.
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Affiliation(s)
- Wei Zhang
- School of Electronic Engineering, Changzhou College of Information Technology, China.
| | - Jiao Chen
- Department of Intelligent Equipment, Changzhou College of Information Technology, China
| | - Ling Xie
- Changzhou University Huaide College, China
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Thanasukarn V, Prajumwongs P, Muangritdech N, Loilome W, Namwat N, Klanrit P, Wangwiwatsin A, Charoenlappanit S, Jaresitthikunchai J, Roytrakul S, Titapun A. Discovery of novel serum peptide biomarkers for cholangiocarcinoma recurrence through MALDI-TOF MS and LC-MS/MS peptidome analysis. Sci Rep 2025; 15:2582. [PMID: 39833435 PMCID: PMC11746940 DOI: 10.1038/s41598-025-87124-2] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Grants] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/06/2024] [Accepted: 01/16/2025] [Indexed: 01/22/2025] Open
Abstract
Cholangiocarcinoma (CCA) is an aggressive cancer originating from bile duct epithelial cells, with a high rate of recurrence following surgical resection. Recurrence is categorized as early linked to aggressive tumor biology than late recurrence. This study aimed to identify novel peptide mass fingerprints (PMFs) and potential biomarker panels in the serum of CCA patients with early and late recurrence using mass spectrometry. Serum samples of 81 CCA patients were analyzed using MALDI-TOF MS and LC-MS/MS, with statistical analysis correlating peptide profiles with clinical outcomes like disease-free survival (DFS) and overall survival (OS). A 365-day DFS cut-off effectively distinguished early from late recurrence, with early recurrence linked to poorer survival outcomes. The PMFs from MALDI-TOF MS differentiated recurrence types based on specific mass signatures. LC-MS/MS analysis identified 95 peptides associated with cancer progression in early recurrence and 60 in late recurrence. Distinct protein associations were found: ATR, POLA1, BLM, SP100, and PPP1R15A for early recurrence, and SERPINA1, TGFB2, SERPING1, and CAD for late recurrence, with strong interactions with chemotherapeutic drugs. This study successfully demonstrated the use of PMFs for rapid discrimination between early and late recurrence in CCA and identified potential serum peptide biomarkers to improve accuracy in recurrence classification.
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Affiliation(s)
- Vasin Thanasukarn
- Department of Surgery, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
| | - Piya Prajumwongs
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
| | - Nattha Muangritdech
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
| | - Watcharin Loilome
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
- Department of Systems Biosciences and Computational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand
| | - Nisana Namwat
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
- Department of Systems Biosciences and Computational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand
| | - Poramate Klanrit
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
- Department of Systems Biosciences and Computational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand
| | - Arporn Wangwiwatsin
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand
- Department of Systems Biosciences and Computational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand
| | - Sawanya Charoenlappanit
- Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani, Thailand
| | - Janthima Jaresitthikunchai
- Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani, Thailand
| | - Sittiruk Roytrakul
- Functional Proteomics Technology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani, Thailand
| | - Attapol Titapun
- Department of Surgery, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.
- Cholangiocarcinoma Research Institute, Khon Kaen University, Khon Kaen, Thailand.
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Sousa P, Silva L, Luís C, Câmara JS, Perestrelo R. MALDI-TOF MS: A Promising Analytical Approach to Cancer Diagnostics and Monitoring. SEPARATIONS 2023; 10:453. [DOI: 10.3390/separations10080453] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Indexed: 01/03/2025] Open
Abstract
Cancer remains the second most common cause of death after cardiovascular diseases, accounting for nearly 10 million deaths in 2020. Although the incidence of cancer increases considerably with age, the cancer burden can also be reduced and have a high chance of cure through early detection, appropriate treatment, and care of patients. The development of high-throughput analytical approaches, like matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), contributes to identifying a pool of proteins/peptides as putative biomarkers for the early detection, diagnosis, and tumor progression. The purpose of the current review is to present an updated outline of recent proteome/peptidome research to establish putative cancer biomarkers using MALDI-TOF MS and highlight the applicability of statistical analysis in the oncology field. The pros and cons of MALDI-TOF MS application on cancer diagnostics and monitoring will be discussed, as well as compared with tandem mass spectrometry (MS/MS)-based proteomics (e.g., liquid chromatography–tandem mass spectrometry). In addition, pre-analytical (e.g., sample quality control) and analytical (e.g., sample pre-treatment, instrumental analytical conditions) properties that influence the robustness of MALDI-TOF MS data will be also discussed.
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Affiliation(s)
- Patrícia Sousa
- CQM—Centro de Química da Madeira, Universidade da Madeira, Campus da Penteada, 9020-105 Funchal, Portugal
| | - Laurentina Silva
- Hospital Dr. Nélio Mendonça, SESARAM, EPERAM—Serviço de Saúde da Região Autónoma da Madeira, Avenida Luís de CamõesK, 9004-514 Funchal, Portugal
| | - Catarina Luís
- CQM—Centro de Química da Madeira, Universidade da Madeira, Campus da Penteada, 9020-105 Funchal, Portugal
| | - José S. Câmara
- CQM—Centro de Química da Madeira, Universidade da Madeira, Campus da Penteada, 9020-105 Funchal, Portugal
- Departamento de Química, Faculdade de Ciências Exatas e Engenharia, Universidade da Madeira, Campus da Penteada, 9020-105 Funchal, Portugal
| | - Rosa Perestrelo
- CQM—Centro de Química da Madeira, Universidade da Madeira, Campus da Penteada, 9020-105 Funchal, Portugal
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Lavigne A, Géhin T, Gilquin B, Jousseaume V, Veillerot M, Botella C, Chevalier C, Jamois C, Chevolot Y, Phaner-Goutorbe M, Yeromonahos C. Effect of Silane Monolayers and Nanoporous Silicon Surfaces on the Matrix-Assisted Laser Desorption Ionization Mass Spectrometry Detection of Sepsis Metabolites Biomarkers Mixed in Solution. ACS OMEGA 2023; 8:28898-28909. [PMID: 37576693 PMCID: PMC10413469 DOI: 10.1021/acsomega.3c04266] [Citation(s) in RCA: 0] [Impact Index Per Article: 0] [Reference Citation Analysis] [Abstract] [Grants] [Track Full Text] [Download PDF] [Figures] [Subscribe] [Scholar Register] [Received: 06/15/2023] [Accepted: 07/07/2023] [Indexed: 08/15/2023]
Abstract
Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-ToF MS) is a promising strategy for clinical diagnosis based on metabolite detection. However, several bottlenecks (such as the lack of reproducibility in analysis, the presence of an important background in low-mass range, and the lack of organic matrix for some molecules) prevent its transfer to clinical cases. These limitations can be addressed by using nanoporous silicon surfaces chemically functionalized with silane monolayers. In the present study, sepsis metabolite biomarkers were used to investigate the effects of silane monolayers and porous silicon substrates on MALDI-ToF MS analysis (signal-to-noise value (S/N), relative standard deviation of the S/N of triplicate samples (STDmean), and intra-substrates uniformity). Also, the impact of the physicochemical properties of metabolites, with different isoelectric points and hydrophobic-hydrophilic balances, was assessed. Four different silane molecules, with various alkyl chain lengths and head-group charges, were self-assembled in monolayers on plane and porous silicon surfaces. Their surface coverage and conformity were investigated by X-ray photoelectron spectroscopy (XPS) and time-of-flight secondary ion mass spectrometry (ToF-SIMS). The seven metabolites detected on the stainless-steel target plate (lysophosphatidylcholine, caffeine, phenylalanine, creatinine, valine, arginine, and glycerophosphocholine) are also detected on the silanized and bare, plane and porous silicon surfaces. Moreover, two metabolites, glycine and alanine, which are not detected on the stainless-steel target plate, are detected on all silanized surfaces, except glycine which is not detected on CH3 short-modified porous silicon and on the bare plane silicon substrate. In addition, whatever the metabolites (except phenylalanine and valine), at least one of the silicon surfaces allows to increase the S/N value in comparison with the stainless-steel target plate. Also, the heterogeneity of matrix crystallization features is linked to the STDmean which is poor on the NH3+ monolayer on plane substrate and better on the NH3+ monolayer on porous substrate, for most of the metabolites. Nevertheless, matrix crystallization features are not sufficient to systematically get high STDmean and uniformity in MALDI-ToF MS analysis. Indeed, the physicochemical properties of metabolites and surfaces, limitations in metabolite extraction from the pores, and improvement in metabolite desorption due to the pores are shown to significantly impact MS analysis. In particular, in the case of the most hydrophobic metabolites studied, the highest S/N values and the best STDmean and uniformity (the lowest values) are reached by using porous substrates, while in the case of the most hydrophilic metabolites studied, plane substrates demonstrated the highest S/N and the lowest STDmean. No clear trend of surface chemistry was evidenced.
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Affiliation(s)
- Antonin Lavigne
- Univ
Lyon, Ecole Centrale de Lyon, CNRS, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
| | - Thomas Géhin
- Univ
Lyon, CNRS, Ecole Centrale de Lyon, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
| | - Benoît Gilquin
- Univ
Grenoble Alpes, CEA, LETI, F-38000 Grenoble, France
| | | | - Marc Veillerot
- Univ
Grenoble Alpes, CEA, LETI, F-38000 Grenoble, France
| | - Claude Botella
- Univ
Lyon, CNRS, Ecole Centrale de Lyon, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
| | - Céline Chevalier
- Univ
Lyon, INSA Lyon, CNRS, Ecole Centrale de Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69621 Villeurbanne Cedex, France
| | - Cécile Jamois
- Univ
Lyon, INSA Lyon, CNRS, Ecole Centrale de Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69621 Villeurbanne Cedex, France
| | - Yann Chevolot
- Univ
Lyon, CNRS, Ecole Centrale de Lyon, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
| | - Magali Phaner-Goutorbe
- Univ
Lyon, Ecole Centrale de Lyon, CNRS, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
| | - Christelle Yeromonahos
- Univ
Lyon, Ecole Centrale de Lyon, CNRS, INSA Lyon, Université Claude
Bernard Lyon 1, CPE Lyon, INL, UMR5270, 69134 Ecully Cedex, France
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Li C, Xiao J, Wu S, Liu L, Zeng X, Zhao Q, Zhang Z. Clinical application of serum-based proteomics technology in human tumor research. Anal Biochem 2023; 663:115031. [PMID: 36580994 DOI: 10.1016/j.ab.2022.115031] [Citation(s) in RCA: 4] [Impact Index Per Article: 2.0] [Reference Citation Analysis] [Abstract] [Key Words] [MESH Headings] [Track Full Text] [Journal Information] [Subscribe] [Scholar Register] [Received: 10/28/2022] [Revised: 12/20/2022] [Accepted: 12/24/2022] [Indexed: 12/27/2022]
Abstract
The rapid development of proteomics technology in the past decades has led to further human understanding of tumor research, and in some ways, the technology plays a very important supporting role in the early detection of tumors. Human serum has been shown to contain a variety of proteins closely related to life activities, and the dynamic change in proteins can often reflect the physiological and pathological conditions of the body. Serum has the advantage of easy extraction, so the application of proteomics technology in serum has become a hot spot and frontier area for the study of malignant tumors. However, there are still many difficulties in the standardized use of proteomic technologies, which inevitably limit the clinical application of proteomic technologies due to the heterogeneity of human proteins leading to incomplete whole proteome populations, in addition to most serum protein markers being now not highly specific in aiding the early detection of tumors. Nevertheless, further development of proteomics technologies will greatly increase our understanding of tumor biology and help discover more new tumor biomarkers with specificity that will enable medical technology.
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Affiliation(s)
- Chen Li
- Department of Pathology, The First Affiliated Hospital of University of South China, Hunan, Hengyang, 421001, Hunan Province, China
| | - Juan Xiao
- Department of Otorhinolaryngology, The Second Affiliated Hospital of University of South China, Hunan, Hengyang, 421001, Hunan Province, China
| | - Shihua Wu
- Department of Pathology, The Second Hospital of Shaoyang College, Hunan, Shaoyang, 422000, Hunan Province, China
| | - Lu Liu
- Department of Pathology, The First Affiliated Hospital of University of South China, Hunan, Hengyang, 421001, Hunan Province, China
| | - Xuemei Zeng
- Cancer Research Institute of Hengyang Medical College, University of South China, Key Laboratory of Cancer Cellular and Molecular Pathology in Hunan Province, Hunan, Hengyang, 421001, China
| | - Qiang Zhao
- Department of Pathology, The First Affiliated Hospital of University of South China, Hunan, Hengyang, 421001, Hunan Province, China.
| | - Zhiwei Zhang
- Department of Pathology, The First Affiliated Hospital of University of South China, Hunan, Hengyang, 421001, Hunan Province, China; Cancer Research Institute of Hengyang Medical College, University of South China, Key Laboratory of Cancer Cellular and Molecular Pathology in Hunan Province, Hunan, Hengyang, 421001, China.
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Punetha A, Kotiya D. Advancements in Oncoproteomics Technologies: Treading toward Translation into Clinical Practice. Proteomes 2023; 11:2. [PMID: 36648960 PMCID: PMC9844371 DOI: 10.3390/proteomes11010002] [Citation(s) in RCA: 4] [Impact Index Per Article: 2.0] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/06/2022] [Revised: 01/03/2023] [Accepted: 01/04/2023] [Indexed: 01/12/2023] Open
Abstract
Proteomics continues to forge significant strides in the discovery of essential biological processes, uncovering valuable information on the identity, global protein abundance, protein modifications, proteoform levels, and signal transduction pathways. Cancer is a complicated and heterogeneous disease, and the onset and progression involve multiple dysregulated proteoforms and their downstream signaling pathways. These are modulated by various factors such as molecular, genetic, tissue, cellular, ethnic/racial, socioeconomic status, environmental, and demographic differences that vary with time. The knowledge of cancer has improved the treatment and clinical management; however, the survival rates have not increased significantly, and cancer remains a major cause of mortality. Oncoproteomics studies help to develop and validate proteomics technologies for routine application in clinical laboratories for (1) diagnostic and prognostic categorization of cancer, (2) real-time monitoring of treatment, (3) assessing drug efficacy and toxicity, (4) therapeutic modulations based on the changes with prognosis and drug resistance, and (5) personalized medication. Investigation of tumor-specific proteomic profiles in conjunction with healthy controls provides crucial information in mechanistic studies on tumorigenesis, metastasis, and drug resistance. This review provides an overview of proteomics technologies that assist the discovery of novel drug targets, biomarkers for early detection, surveillance, prognosis, drug monitoring, and tailoring therapy to the cancer patient. The information gained from such technologies has drastically improved cancer research. We further provide exemplars from recent oncoproteomics applications in the discovery of biomarkers in various cancers, drug discovery, and clinical treatment. Overall, the future of oncoproteomics holds enormous potential for translating technologies from the bench to the bedside.
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Affiliation(s)
- Ankita Punetha
- Department of Microbiology, Biochemistry and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers University, 225 Warren St., Newark, NJ 07103, USA
| | - Deepak Kotiya
- Department of Pharmacology and Nutritional Sciences, University of Kentucky, 900 South Limestone St., Lexington, KY 40536, USA
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Li D, Yi J, Han G, Qiao L. MALDI-TOF Mass Spectrometry in Clinical Analysis and Research. ACS MEASUREMENT SCIENCE AU 2022; 2:385-404. [PMID: 36785658 PMCID: PMC9885950 DOI: 10.1021/acsmeasuresciau.2c00019] [Citation(s) in RCA: 53] [Impact Index Per Article: 17.7] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Subscribe] [Scholar Register] [Received: 03/31/2022] [Revised: 07/15/2022] [Accepted: 07/15/2022] [Indexed: 05/04/2023]
Abstract
In the decade after being awarded the Nobel Prize in Chemistry in 2002, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been widely used as an analytical chemistry tool for the detection of large and small molecules (e.g., polymers, proteins, peptides, nucleic acids, amino acids, lipids, etc.) and for clinical analysis and research (e.g., pathogen identification, genetic disorders screening, cancer diagnosis, etc.). In view of the fast development of MALDI-TOF MS in clinical usage, this review systematically summarizes the most important applications of MALDI-TOF MS in clinical analysis and research by analyzing MALDI TOF MS-related reviews collected in the Web of Science database. On the basis of the analysis of keyword co-occurrence of over 2000 review articles, four themes consisting of "pathogen identification", "disease diagnosis", "nucleic acids analysis", and "small molecules analysis" were found. For each theme, the review further outlined their application implications, analytical methods, and systems as well as limitations that need to be addressed. Overall, the review summarizes and elaborates on the clinical applications of MALDI-TOF MS, providing a comprehensive picture for researchers embarking on MALDI TOF MS-related clinical analysis and research.
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Zhang W, Li D, Xu B, Xu L, Lyu Q, Liu X, Li Z, Zhang J, Sun W, Ma Q, Qiao L, Liao P. Serum peptidome profiles immune response of COVID-19 Vaccine administration. Front Immunol 2022; 13:956369. [PMID: 36091008 PMCID: PMC9450691 DOI: 10.3389/fimmu.2022.956369] [Citation(s) in RCA: 3] [Impact Index Per Article: 1.0] [Reference Citation Analysis] [Abstract] [MESH Headings] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 05/30/2022] [Accepted: 08/01/2022] [Indexed: 11/13/2022] Open
Abstract
BackgroundCoronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has caused significant loss of life and property. In response to the serious pandemic, recently developed vaccines against SARS-CoV-2 have been administrated to the public. Nevertheless, the research on human immunization response against COVID-19 vaccines is insufficient. Although much information associated with vaccine efficacy, safety and immunogenicity has been reported by pharmaceutical companies based on laboratory studies and clinical trials, vaccine evaluation needs to be extended further to better understand the effect of COVID-19 vaccines on human beings.MethodsWe performed a comparative peptidome analysis on serum samples from 95 participants collected at four time points before and after receiving CoronaVac. The collected serum samples were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the serum peptides, and also subjected to humoral and cellular immune response analyses to obtain typical immunogenicity information.ResultsSignificant difference in serum peptidome profiles by MALDI-TOF MS was observed after vaccination. By supervised statistical analysis, a total of 13 serum MALDI-TOF MS feature peaks were obtained on day 28 and day 42 of vaccination. The feature peaks were identified as component C1q receptor, CD59 glycoprotein, mannose-binding protein C, platelet basic protein, CD99 antigen, Leucine-rich alpha-2-glycoprotein, integral membrane protein 2B, platelet factor 4 and hemoglobin subunits. Combining with immunogenicity analysis, the study provided evidence for the humoral and cellular immune responses activated by CoronaVac. Furthermore, we found that it is possible to distinguish neutralizing antibody (NAbs)-positive from NAbs-negative individuals after complete vaccination using the serum peptidome profiles by MALDI-TOF MS together with machine learning methods, including random forest (RF), partial least squares-discriminant analysis (PLS-DA), linear support vector machine (SVM) and logistic regression (LR).ConclusionsThe study shows the promise of MALDI-TOF MS-based serum peptidome analysis for the assessment of immune responses activated by COVID-19 vaccination, and discovered a panel of serum peptides biomarkers for COVID-19 vaccination and for NAbs generation. The method developed in this study can help not only in the development of new vaccines, but also in the post-marketing evaluation of developed vaccines.
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Affiliation(s)
- Wenjia Zhang
- Department of Clinical Laboratory, Chongqing General Hospital, Chongqing, China
| | - Dandan Li
- Department of Chemistry, Fudan University, Shanghai, China
| | - Bin Xu
- Bioyong Technologics, Inc., Beijing, China
| | - Lanlan Xu
- Department of Clinical Laboratory, Chongqing General Hospital, Chongqing, China
| | - Qian Lyu
- Bioyong Technologics, Inc., Beijing, China
| | - Xiangyi Liu
- Department of Laboratory Medicine, Beijing Tongren Hospital, Capital Medical University, Beijing, China
| | - Zhijie Li
- Department of Clinical Laboratory, Chongqing General Hospital, Chongqing, China
| | - Jian Zhang
- State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing, China
| | - Wei Sun
- State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing, China
| | - Qingwei Ma
- Bioyong Technologics, Inc., Beijing, China
| | - Liang Qiao
- Department of Chemistry, Fudan University, Shanghai, China
- *Correspondence: Pu Liao, ; Liang Qiao,
| | - Pu Liao
- Department of Clinical Laboratory, Chongqing General Hospital, Chongqing, China
- *Correspondence: Pu Liao, ; Liang Qiao,
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Wang HJ, Xie YB, Zhang PJ, Jiang T. Evaluation of the diagnostic value of serum-based proteomics for colorectal cancer. World J Gastrointest Oncol 2022; 14:1562-1573. [PMID: 36160749 PMCID: PMC9412932 DOI: 10.4251/wjgo.v14.i8.1562] [Citation(s) in RCA: 1] [Impact Index Per Article: 0.3] [Reference Citation Analysis] [Abstract] [Key Words] [Track Full Text] [Download PDF] [Journal Information] [Submit a Manuscript] [Subscribe] [Scholar Register] [Received: 03/08/2022] [Revised: 04/13/2022] [Accepted: 07/18/2022] [Indexed: 02/05/2023] Open
Abstract
BACKGROUND Colorectal cancer (CRC) is a highly malignant cancer with a high incidence and mortality in China. It is urgent to find a diagnostic marker with higher sensitivity and specificity than the traditional approaches for CRC diagnosis.
AIM To provide new ideas for the diagnosis of CRC based on serum proteomics.
METHODS Specimens from 83 healthy people, 62 colon polyp (CRP) patients, and 101 CRC patients were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The diagnostic value of the profiles of differentially expressed proteins was then analyzed.
RESULTS Compared with the healthy control group, CRC patients had elevated expression of 5 proteins and reduced expression of 14 proteins. The area under the curve (AUC) for a differentially expressed protein with a mass-to-charge ratio of 2022.34 was the largest; the AUC was 0.843, which was higher than the AUC of 0.717 observed with carcinoembryonic antigen (CEA), and the sensitivity and specificity of this identified marker were 75.3% and 79.5%, respectively. After cross-validation, the accuracy of diagnosis using levels of this differentially expressed protein was 82.37%. Compared with the CRP group, the expression of 3 proteins in the serum of CRC patients was elevated and 11 proteins were expressed at reduced levels. Proteins possessing mass-to-charge ratio values of 2899.38 and 877.3 were selected to establish a classification tree model. The results showed that the accuracy of CRC diagnosis was 89.5%, the accuracy of CRP diagnosis was 81.6%, and the overall accuracy of this approach was 86.3%. The overall sensitivity and specificity of diagnosis using the proteomics approach were 81.8% and 66.75%, respectively. The sensitivities and specificities of diagnoses based on CEA and carbohydrate antigen 19-9 expression were 55.6% and 91.3% and 65.4% and 65.2%, respectively.
CONCLUSION We demonstrated that serum proteomics may be helpful for the detection of CRC, and it may assist clinical practice for CRC diagnosis.
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Affiliation(s)
- Hui-Juan Wang
- Department of Respiratory and Critical Care Medicine, Beijing Chao-Yang Hospital, Beijing Institute of Respiratory Medicine, Capital Medical University, Beijing 100020, China
| | - Yi-Bin Xie
- Department of Pancreatic and Gastric Surgery, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100021, China
| | - Peng-Jun Zhang
- Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education/Beijing), Interventional Therapy Department, Peking University Cancer Hospital and Institute, Beijing 100142, China
| | - Tao Jiang
- Medical Innovation Research Division of Chinese PLA General Hospital, Beijing 100853, China
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Li C, Chu S, Tan S, Yin X, Jiang Y, Dai X, Gong X, Fang X, Tian D. Towards Higher Sensitivity of Mass Spectrometry: A Perspective From the Mass Analyzers. Front Chem 2021; 9:813359. [PMID: 34993180 PMCID: PMC8724130 DOI: 10.3389/fchem.2021.813359] [Citation(s) in RCA: 58] [Impact Index Per Article: 14.5] [Reference Citation Analysis] [Abstract] [Key Words] [Grants] [Track Full Text] [Download PDF] [Figures] [Journal Information] [Subscribe] [Scholar Register] [Received: 11/11/2021] [Accepted: 12/06/2021] [Indexed: 01/12/2023] Open
Abstract
Mass spectrometry (MS) is one of the most widely used analytical techniques in many fields. Recent developments in chemical and biological researches have drawn much attention to the measurement of substances with low abundances in samples. Continuous efforts have been made consequently to further improve the sensitivity of MS. Modifications on the mass analyzers of mass spectrometers offer a direct, universal and practical way to obtain higher sensitivity. This review provides a comprehensive overview of the latest developments in mass analyzers for the improvement of mass spectrometers' sensitivity, including quadrupole, ion trap, time-of-flight (TOF) and Fourier transform ion cyclotron (FT-ICR), as well as different combinations of these mass analyzers. The advantages and limitations of different mass analyzers and their combinations are compared and discussed. This review provides guidance to the selection of suitable mass spectrometers in chemical and biological analytical applications. It is also beneficial to the development of novel mass spectrometers.
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Affiliation(s)
- Chang Li
- College of Instrumentation & Electrical Engineering, Jilin University, Changchun, China
| | - Shiying Chu
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Siyuan Tan
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Xinchi Yin
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - You Jiang
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Xinhua Dai
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Xiaoyun Gong
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Xiang Fang
- Technology Innovation Center of Mass Spectrometry for State Market Regulation, Center for Advanced Measurement Science, National Institute of Metrology, Beijing, People’s Republic ofChina
| | - Di Tian
- College of Instrumentation & Electrical Engineering, Jilin University, Changchun, China
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