Mass Spectrometry Reviews最新文献

{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 2","pages":"156-157"},"PeriodicalIF":6.6,"publicationDate":"2025-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148121569","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"45 2","pages":"156-157"},"PeriodicalIF":6.6,"publicationDate":"2025-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148094434","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advances in the Mechanistic Understanding of Matrix-Assisted Laser Desorption/Ionization In-Source Decay Mass Spectrometry for Peptides and Proteins: Electron Transfer Reaction as the Initiating Step of Fragmentation.","authors":"Daiki Asakawa","doi":"10.1002/mas.70006","DOIUrl":"https://doi.org/10.1002/mas.70006","url":null,"abstract":"<p><p>Because matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) induces selective cleavage on the peptide backbone, this technique allows reliable identification of peptides and proteins. In the last 15 years, several new matrices have been developed that more efficiently induce MALDI-ISD, opening new research avenues. Fragmentation of peptides by MALDI-ISD can be divided into two categories: reducing and oxidizing matrices induce selective cleavage of N-Cα and Cα-C bonds, respectively. Regarding the dissociation mechanism, MALDI-ISD was believed, until recently, to be initiated by \"hydrogen atom\" transfer between an analyte peptide and the matrix. Based on this hypothesis, the origin of the hydrogen atoms would be the aniline group of the matrix in MALDI with a reducing matrix and the amide nitrogen of the peptide backbone in MALDI-ISD with an oxidizing matrix. MALDI-ISD involves homolytic cleavage of N-H bonds, though the N-H bond is generally stronger than O-H and C-H bonds. Notably, mass spectrometry experiments cannot distinguish between \"hydrogen atom transfer\" and \"electron transfer and subsequent proton transfer.\" Recent well-designed experiments and quantum chemistry calculations have strongly suggested that electron transfer between the peptide and matrix is likely to be the initial step of the MALDI-ISD process. Reducing and oxidizing matrices for MALDI-ISD induce fragmentation through peptide radical anions and cations, respectively. The generated fragment ions and radicals subsequently undergo reactions within the MALDI plume, leading to the formation of stable even-electron ions that are detectable in the mass spectrum. As a result, MALDI-ISD fragments are observed as both positively and negatively charged ions, despite MALDI-ISD entailing the fragmentation of peptide radical anions and cations. The proposed mechanism offers a robust framework for understanding the MALDI-ISD process. A more comprehensive understanding of this process is essential to fully harness the potential of the MALDI-ISD technique and would pave the way for further development of methodologies advancing the field of analytical chemistry based on finding new matrices.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.6,"publicationDate":"2025-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Analytical Approaches to Address Challenges in the Analysis of Cannabinoids in Vascular Matrices Using Mass Spectrometry.","authors":"Radwa Mahmoud, Robert B Laprairie, Anas El-Aneed","doi":"10.1002/mas.70005","DOIUrl":"https://doi.org/10.1002/mas.70005","url":null,"abstract":"<p><p>Phytocannabinoids are bioactive metabolites derived from the Cannabis sativa plant. They have garnered attention due to their recreational uses and therapeutic potential. Although various analytical strategies have been employed for their analysis, mass spectrometry (MS) coupled to chromatographic separation is superior due to its sensitivity and selectivity. Various MS-based strategies, namely Gas chromatography (GC-MS) and liquid chromatography - MS (LC-MS) are reviewed with focus on the analysis of phytocannabinoids in vascular matrices. These include plasma, serum, whole blood, and dried blood spots (DBS). Applications, advantages and challenges associated with each MS strategy in vascular matrices are evaluated and critically discussed. In addition, the review outlines the challenges in DBS spot analysis, such as hematocrit bias, versus plasma/serum and whole blood processing, which involves protein removal, extraction and cleanup steps.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":" ","pages":""},"PeriodicalIF":6.6,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144937358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pivotal Role of Mass Spectrometry for the Assessment of Exposure to Reactive Chemical Contaminants: From the Exposome to the Adductome","authors":"Laurent Debrauwer,&nbsp;Loic Mervant,&nbsp;Olivier Laprevote,&nbsp;Emilien L. Jamin","doi":"10.1002/mas.21917","DOIUrl":"10.1002/mas.21917","url":null,"abstract":"<div>\u0000 \u0000 <p>A large part of the Human chemical exposome is now well characterized, and its health effects has been widely documented, although precise causal links remain difficult to establish. In parallel, genetic factors only were shown to contribute less than 30% to various pathologies. Therefore, environmental factors may represent the predominant cause of chronic diseases. Mass Spectrometry has been established for many years as a main “gold standard” in this field due to its performances both in sensitivity and selectivity. However, some unstable or highly reactive compounds may escape their detection in the biological samples because of their short half-life although some of their stable metabolites, if any, can be used for the exposure assessment. These electrophilic molecules are known to bind covalently to nucleophilic molecules in the body to form what are commonly called adducts. The study of adducts formed with DNA, proteins or with glutathione, nowadays called adductomics, can provide additional toxicologically relevant information in biomonitoring studies. This review describes this particular part of the reactive exposome and the related mass spectrometric methods developed therein. Three dedicated parts of this review are devoted to the contribution of mass spectrometry respectively to the assessment of DNA modifications, protein modifications, and reaction with glutathione.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"830-849"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142764737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Photoaffinity labeling coupled to MS to identify peptide biological partners: Secondary reactions, for better or for worse?","authors":"Astrid Walrant,&nbsp;Emmanuelle Sachon","doi":"10.1002/mas.21880","DOIUrl":"10.1002/mas.21880","url":null,"abstract":"<p>Affinity photolabeling is a smart method to study noncovalent and transient interactions and provide a submolecular picture of the contacts between interacting partners. In this review, we will focus on the identification of peptide partners using photoaffinity labeling coupled to mass spectrometry in different contexts such as in vitro with a purified potential partner, in model systems such as model membranes, and with live cells using both targeted and nontargeted proteomics studies. Different biological partners will be described, among which glycoconjugates, oligonucleotides, peptides, proteins, and lipids, with the photoreactive label inserted either on the peptide of interest or on the potential partner. Particular attention will be paid to the observation and characterization of specific rearrangements following the photolabeling reaction, which can help characterize photoadducts and provide a better understanding of the interacting systems and environment.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"715-756"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21880","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140584392","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protein analysis by desorption electrospray ionization mass spectrometry","authors":"Andre R. Venter","doi":"10.1002/mas.21900","DOIUrl":"10.1002/mas.21900","url":null,"abstract":"<p>This review presents progress made in the ambient analysis of proteins, in particular by desorption electrospray ionization-mass spectrometry (DESI-MS). Related ambient ionization techniques are discussed in comparison to DESI-MS only to illustrate the larger context of protein analysis by ambient ionization mass spectrometry. The review describes early and current approaches for the analysis of undigested proteins, native proteins, tryptic digests, and indirect protein determination through reporter molecules. Applications to mass spectrometry imaging for protein spatial distributions, the identification of posttranslational modifications, determination of binding stoichiometries, and enzymatic transformations are discussed. The analytical capabilities of other ambient ionization techniques such as LESA and nano-DESI currently exceed those of DESI-MS for in situ surface sampling of intact proteins from tissues. This review shows, however, that despite its many limitations, DESI-MS is making valuable contributions to protein analysis. The challenges in sensitivity, spatial resolution, and mass range are surmountable obstacles and further development and improvements to DESI-MS is justified.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"757-772"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141756049","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ion Source Complementarity for Characterization of Complex Organic Mixtures Using Fourier Transform Mass Spectrometry: A Review","authors":"Charlotte Mase,&nbsp;Maxime Sueur,&nbsp;Hélène Lavanant,&nbsp;Christopher Paul Rüger,&nbsp;Pierre Giusti,&nbsp;Carlos Afonso","doi":"10.1002/mas.21910","DOIUrl":"10.1002/mas.21910","url":null,"abstract":"<p>Complex organic mixtures are found in many areas of research, such as energy, environment, health, planetology, and cultural heritage, to name but a few. However, due to their complex chemical composition, which holds an extensive potential of information at the molecular level, their molecular characterization is challenging. In mass spectrometry, the ionization step is the key step, as it determines which species will be detected. This review presents an overview of the main ionization sources employed to characterize these kinds of samples in Fourier transform mass spectrometry (FT-MS), namely electrospray (ESI), atmospheric pressure photoionization (APPI), atmospheric pressure chemical ionization (APCI), atmospheric pressure laser ionization (APLI), and (matrix-assisted) laser desorption ionization ((MA)LDI), and their complementarity in the characterization of complex organic mixtures. First, the ionization techniques are examined in the common direct introduction (DI) usage. Second, these approaches are discussed in the context of coupling chromatographic techniques such as gas chromatography, liquid chromatography, and supercritical fluid chromatography.</p>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"808-829"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/mas.21910","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142454324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Richard B. Cole—Reminiscences Upon the Occasion of His Retirement From Sorbonne Université","authors":"André M. Striegel","doi":"10.1002/mas.21936","DOIUrl":"10.1002/mas.21936","url":null,"abstract":"","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"670-672"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143956507","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advances in Single Particle Mass Analysis","authors":"Szu-Hsueh Lai,&nbsp;Sylvain Maclot,&nbsp;Rodolphe Antoine,&nbsp;Christophe D. Masselon","doi":"10.1002/mas.21920","DOIUrl":"10.1002/mas.21920","url":null,"abstract":"<div>\u0000 \u0000 <p>Single particle mass analysis methods allow the measurement and characterization of individual nanoparticles, viral particles, as well as biomolecules like protein aggregates and complexes. Several key benefits are associated with the ability to analyze individual particles rather than bulk samples, such as high sensitivity and low detection limits, and virtually unlimited dynamic range, as this figure of merit strictly depends on analysis time. However, data processing and interpretation of single particle data can be complex, often requiring advanced algorithms and machine learning approaches. In addition, particle ionization, transfer, and detection efficiency can be limiting factors for certain types of analytes. Ongoing developments in the field aim to address these challenges and expand the capabilities of single particle mass analysis techniques. Charge detection mass spectrometry is a single particle version of mass spectrometry in which the charge (z) is determine independently from <i>m/z</i>. Nano-electromechanical resonator mass analysis relies on changes in a nanoscale device's resonance frequency upon deposition of a particle to directly derive its inertial mass. Mass photometry uses interferometric video-microscopy to derive particle mass from the intensity of the scattered light. A common feature of these approaches is the acquisition of single particle data, which can be filtered and concatenated in the form of a particle mass distribution. In the present article, dedicated to our honored colleague Richard Cole, we cover the latest technological advances and applications of these single particle mass analysis approaches.</p>\u0000 </div>","PeriodicalId":206,"journal":{"name":"Mass Spectrometry Reviews","volume":"44 5","pages":"850-869"},"PeriodicalIF":6.6,"publicationDate":"2025-08-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142793968","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}