Journal of Mass Spectrometry最新文献

{"title":"A Top Solvent-Additive-Ionization Technique Combination for Pesticides Direct Infusion MS Analysis","authors":"Darko Anđelković,&nbsp;Milica Branković","doi":"10.1002/jms.5092","DOIUrl":"10.1002/jms.5092","url":null,"abstract":"<div>\u0000 \u0000 <p>The leading type of ionization technique in mass spectrometry analyses is the ionization at atmospheric pressure. The aim of this study was to assess ESI and APCI ionization efficiency of pesticides introduced to the MS source in four organic phases, non-doped and doped with formic acid and ammonium formate. Ionization efficiency in modified ESI and APCI, applying in-source sample heating, was also assessed. The study was primarily designed to support non-chromatography-based mass spectrometry pesticides analysis by the direct infusion technique. Evaluation of analysis performances such as calibration performances, detectability, and sensitivity should indicate a top solvent-additive-source combination, leading to the highest ionization efficiency and lowest analytes detection limits.</p>\u0000 </div>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142256195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Absolute Quantification of Glutathione Using Top-Hat Optics for IR-MALDESI Mass Spectrometry Imaging","authors":"Emily R. Bruce,&nbsp;Russell R. Kibbe,&nbsp;Emily C. Hector,&nbsp;David C. Muddiman","doi":"10.1002/jms.5091","DOIUrl":"https://doi.org/10.1002/jms.5091","url":null,"abstract":"<p>Infrared matrix-assisted laser desorption electrospray ionization (IR-MALDESI) uses an infrared laser to desorb neutral biomolecules with postionization via ESI at atmospheric pressure. The Gaussian profile of the laser with conventional optics results in the heating of adjacent nonablated tissue due to the energy profile being circular. A diffractive optical element (DOE) was incorporated into the optical train to correct for this disadvantage. The DOE produces a top-hat beam profile and square ablation spots, which have uniform energy distributions. Although beneficial to mass spectrometry imaging (MSI), it is unknown how the DOE affects the ability to perform quantitative MSI (qMSI). In this work, we evaluate the performance of the DOE optical train against our conventional optics to define the potential advantages of the top-hat beam profile. Absolute quantification of glutathione (GSH) was achieved by normalizing the analyte of interest to homoglutathione (hGSH), spotting a dilution series of stable isotope labeled glutathione (SIL-GSH), and analyzing by IR-MALDESI MSI with either the conventional optical train or with the DOE incorporated. Statistical comparison indicates that there was no significant difference between the quantification of GSH by the two optical trains as evidenced by similar calibration curves. Results support that both optical trains can be used for qMSI without a change in the ability to carry out absolute quantification but providing the benefits of the top-hat optical train (i.e., flat energy profile and square ablation spots)—for future qMSI studies.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5091","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142244854","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improved Discrimination of Mass Spectral Isomers Using the High-Dimensional Consensus Mass Spectral Similarity Algorithm","authors":"Deborah F. McGlynn,&nbsp;Nirina Rabe Andriamaharavo,&nbsp;Anthony J. Kearsley","doi":"10.1002/jms.5084","DOIUrl":"https://doi.org/10.1002/jms.5084","url":null,"abstract":"<p>This study employs a high-dimensional consensus mass spectral (HDCMS) similarity scoring technique to discriminate isomers collected using an electron ionization mass spectrometer. The HDCMS method was previously introduced and applied to the discrimination of mass spectra of constitutional isomers, methamphetamine and phentermine, collected with direct analysis real-time mass spectrometry (DART-MS). The method formulates the problem of discriminating mass spectra in a mathematical Hilbert space and is hence called “high dimensional.” It requires replicate mass spectra to build a Gaussian model and evaluate the inner products between these functions. The resulting measurement variability is used as a signature by which to discriminate spectra. In this work, HDCMS is tested on electron impact ionization (EI) mass spectra of 7 terpene and terpene-related (C₁₀H₁₆ and C₁₀H₁₄) isomers with experimental retention indices that differ by less than 30 and with traditional cosine similarity scores greater than 0.9, on a scale of 0 to 1, when compared with at least one other compound in the test set. Using identical instrument parameters, 15 replicate gas chromatography–electron ionization–mass spectrometry (GC-EI-MS) spectra of each isomer were collected and separated into distinct library and query sets. The HDCMS algorithm discriminated each isomer, indicating the method's potential. Because the method requires replicate measurements, observations from a simple heuristic study of the number of replicates required to discriminate these isomers is presented. The paper concludes with a discussion of compound discrimination using HDCMS and the benefits and drawbacks of applying the method to EI-MS data.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5084","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142174141","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Clinical glycoprotein mass spectrometry: The future of disease detection and monitoring By Daniel E. Marrero Roche and Kevin Brown Chandler","authors":"Daniel E. Marrero Roche,&nbsp;Kevin Brown Chandler","doi":"10.1002/jms.5086","DOIUrl":"https://doi.org/10.1002/jms.5086","url":null,"abstract":"<p>\u0000 \u0000 <figure>\u0000 <div><picture>\u0000 <source></source></picture><p></p>\u0000 </div>\u0000 </figure></p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5086","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142165428","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular fingerprint by omics-based approaches in saliva from patients affected by SARS-CoV-2 infection","authors":"Gabriella Pinto,&nbsp;Monica Gelzo,&nbsp;Gustavo Cernera,&nbsp;Mariapia Esposito,&nbsp;Anna Illiano,&nbsp;Stefania Serpico,&nbsp;Biagio Pinchera,&nbsp;Ivan Gentile,&nbsp;Giuseppe Castaldo,&nbsp;Angela Amoresano","doi":"10.1002/jms.5082","DOIUrl":"10.1002/jms.5082","url":null,"abstract":"<p>Clinical expression of coronavirus disease 2019 (COVID-19) infectionis widely variable including fatal cases and patients with mild symptoms and a rapid resolution. We studied saliva from 63 hospitalized COVID-19 patients and from 30 healthy controls by integrating large-scale proteomics, peptidomics and targeted metabolomics to assess the biochemical alterations following the infection and to obtain a set of putative biomarkers useful for noninvasive diagnosis. We used an untargeted approach by using liquid chromatography–tandem mass spectrometry (LC–MS/MS) for proteomics and peptidomics analysis and targeted LC–multiple reaction monitoring/MS for the analysis of amino acids. The levels of 77 proteins were significantly different in COVID-19 patients. Among these, seven proteins were found only in saliva from patients with COVID-19, four were up-regulated and three were down-regulated at least five-folds in saliva from COVID-19 patients in comparison to controls. The analysis of proteins revealed a complex balance between pro-inflammatory and anti-inflammatory proteins and a reduced amount of several proteins with immune activity that possibly favours the spreading of the virus. Such reduction could be related to the enhanced activity of endopeptidases induced by the infection that in turn caused an altered balance of free peptides. In fact, on a total of 28 peptides, 22 (80%) were differently expressed in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and control subjects. The multivariate analysis of such peptides permits to obtain a diagnostic algorithm that discriminate the two populations with a high diagnostic efficiency. Among amino acids, only threonine resulted significantly different between COVID-19 patients and controls, while alanine levels were significantly different between COVID-19 patients with different severity. In conclusion, the present study defined a set of molecules to be detected with a quick and easy method based on mass spectrometry tandem useful to reveal biochemical alterations involved in the pathogenesis of such a complex disease. Data are available via ProteomeXchange with identifier PXD045612.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5082","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142125973","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparison of Zybio Kit and saponin in-house method in rapid identification of bacteria from positive blood cultures by EXS2600 matrix-assisted laser desorption ionization time-of-flight mass spectrometry system","authors":"Mislav Peras,&nbsp;Ivana Mareković,&nbsp;Tomislav Kuliš,&nbsp;Manda Markanović,&nbsp;Ana Budimir","doi":"10.1002/jms.5080","DOIUrl":"10.1002/jms.5080","url":null,"abstract":"<p>We evaluated the performance of Zybio EXS2600 matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) (Zybio Inc., Chongqing, China) for the identification of bacteria from positive blood culture (BC) bottles using Blood Culture Positive Sample Pretreatment Kit (Zybio Inc., Chongqing, China) in comparison to an in-house saponin method. Following a positive signal by the BACTEC™ FX system, confirmation of identification was achieved using subcultured growing biomass used for MALDI-TOF MS analysis. A total of 94 positive BC bottles with 97 bacterial isolates were analyzed. The overall identification rates at the genus and species levels for the saponin method were 89.7% (87/97) and 74.2% (72/97), respectively. With the Zybio Kit, 88.7% (86/97) and 80.4% (78/97) of microorganisms were correctly identified to the genus and species levels, respectively. The saponin method identified 65.3% (32/49) of Gram-positive bacteria at the species level, whereas the Zybio Kit achieved a higher species-level identification rate of 79.6% (39/49) (<i>p</i> = 0.1153). The saponin method with additional on-plate formic acid extraction showed a significantly higher overall identification rate in comparison to the saponin method without that step for both genus (87.6% [85/97] vs. 70.1% [68/97], <i>p</i> = 0.0029) and species level (70.1% [68/97] vs. 46.4% [45/97], <i>p</i> = 0.0008). Identification rates of Gram-negative bacteria showed a higher identification rate, however, not statistically significant with additional Zybio Kit protocol step on both genus (85.4% [41/48] vs. 81.3% [39/48], <i>p</i> = 0.5858) and species level (77.1% [37/48] vs. 75% [36/48], <i>p</i> = 0.8120). Zybio Kit could offer an advantage in species-level identification, particularly for Gram-positive bacteria. The inclusion of on-plate formic acid extraction in the saponin method notably enhanced identification at both genus and species levels for Gram-positive bacteria. The extended protocol provided by the Zybio Kit could potentially offer an advantage in the identification of Gram-negative bacteria at both genus and species levels. Enhancements to the Zybio EXS2600 MALDI-TOF instrument software database are necessary.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142125972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dried plasma spot as an innovative approach to therapeutic drug monitoring of apixaban: Development and validation of a novel liquid chromatography-tandem mass spectrometry method","authors":"Alessia Cafaro,&nbsp;Manuela Stella,&nbsp;Giammarco Baiardi,&nbsp;Sebastiano Barco,&nbsp;Federica Pigliasco,&nbsp;Roberto Bandettini,&nbsp;Luca Nanni,&nbsp;Francesca Mattioli,&nbsp;Giuliana Cangemi","doi":"10.1002/jms.5081","DOIUrl":"10.1002/jms.5081","url":null,"abstract":"<div>\u0000 \u0000 \u0000 <section>\u0000 \u0000 <p>Apixaban, a direct oral anticoagulant drug (DOAC), typically does not require routine therapeutic drug monitoring (TDM), yet recent guidelines propose its use in specific clinical scenarios. While various antifactor Xa (anti-FXa) chromogenic assays serve as useful proxies for measuring plasma exposure to apixaban in emergencies, they lack specificity compared with chromatographic methods. This research project is intended to the development and validation of a standardized protocol of liquid chromatography–tandem mass spectrometry (LC–MS/MS) in conformity with the ICH guidelines M10 for the measurement of apixaban in both plasma and dried plasma spots (DPSs). Samples preparation included protein precipitation after the addition of a deuterated internal standard (IS), and the chromatographic separation was carried out on a Thermo Scientific™ Accucore™ Polar Premium column (50 mm × 2.1 mm, i.d. 2.6 m). The newly developed LC–MS/MS method for apixaban mesurement from both plasma and DPS resulted linear over a wide concentration range (31.25–500 ng/mL), accurate, and reproducible without matrix effects, allowing for specific and rapid quantification. Stability was assessed on quality controls and a real sample, allowing the setting up of a robust TDM protocol that was applied to five anonymized plasma samples obtained from adult patients undergoing apixaban treatment at steady-state. In conclusion our novel LC–MS/MS method is adequate for accurate apixaban quantitation from both plasma and DPS matrixes, and may thus facilitate the guidelines suggested implementation of apixaban TDM, even in peripheral hospitals through shipment of DPS at reference laboratories.</p>\u0000 </section>\u0000 </div>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5081","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142073043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Clinical glycoprotein mass spectrometry: The future of disease detection and monitoring","authors":"Daniel E. Marrero Roche,&nbsp;Kevin Brown Chandler","doi":"10.1002/jms.5083","DOIUrl":"10.1002/jms.5083","url":null,"abstract":"<p>Protein glycosylation is the co- and/or post-translational modification of proteins with oligosaccharides (glycans). This process is not template based and can introduce a heterogeneous set of glycan modifications onto substrate proteins. Glycan structures preserve biomolecular information from the cell, with glycoproteins from different cell types and tissues displaying distinct patterns of glycosylation. Several decades of research have revealed that glycan structures also differ between normal physiology and disease. This suggests that the information stored in glycoproteins and glycans can be utilized for disease diagnosis and monitoring. Methods that enable sensitive and site-specific measurement of protein glycosylation in clinical settings, such as nano-flow liquid chromatography tandem mass spectrometry, are therefore essential. The purpose of this perspective is to discuss recent advances in mass spectrometry and the potential of these advances to facilitate the detection and monitoring of disease-specific glycoprotein glycoforms. Glycoproteomics, the system-wide characterization of glycoprotein identity inclusive of site-specific characterization of carbohydrate modifications on proteins, and glycomics, the characterization of glycan structures, will be discussed in this context. Quantitative measurement of glycopeptide markers via parallel reaction monitoring is highlighted. The development of promising glycopeptide markers for autoimmune disease, liver disease, and liver cancer is discussed. Synthetic glycopeptide standards, ambient ionization mass spectrometry, and consideration of glyco-biomarkers in two- and three-dimensional space within tissue will be critical to the advancement of this field. The authors envision a future in which glycoprotein mass spectrometry workflows will be integrated into clinical settings, to aid in the rapid diagnosis and monitoring of disease.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142004418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A deep learning-guided automated workflow in LipidOz for detailed characterization of fungal fatty acid unsaturation by ozonolysis","authors":"Dylan H. Ross,&nbsp;Erin L. Bredeweg,&nbsp;Josie G. Eder,&nbsp;Daniel J. Orton,&nbsp;Meagan C. Burnet,&nbsp;Jennifer E. Kyle,&nbsp;Ernesto S. Nakayasu,&nbsp;Xueyun Zheng","doi":"10.1002/jms.5078","DOIUrl":"10.1002/jms.5078","url":null,"abstract":"<p>Understanding fungal lipid biology and metabolism is critical for antifungal target discovery as lipids play central roles in cellular processes. Nuances in lipid structural differences can significantly impact their functions, making it necessary to characterize lipids in detail to understand their roles in these complex systems. In particular, lipid double bond (DB) locations are an important component of lipid structure that can only be determined using a few specialized analytical techniques. Ozone-induced dissociation mass spectrometry (OzID-MS) is one such technique that uses ozone to break lipid DBs, producing pairs of characteristic fragments that allow the determination of DB positions. In this work, we apply OzID-MS and <i>LipidOz</i> software to analyze the complex lipids of <i>Saccharomyces cerevisiae</i> yeast strains transformed with different fatty acid desaturases from <i>Histoplasma capsulatum</i> to determine the specific unsaturated lipids produced. The automated data analysis in <i>LipidOz</i> made the determination of DB positions from this large dataset more practical, but manual verification for all targets was still time-consuming. The DL model reduces manual involvement in data analysis, but since it was trained using mammalian lipid extracts, the prediction accuracy on yeast-derived data was reduced. We addressed both shortcomings by retraining the DL model to act as a pre-filter to prioritize targets for automated analysis, providing confident manually verified results but requiring less computational time and manual effort. Our workflow resulted in the determination of detailed DB positions and enzymatic specificity.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5078","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141916945","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tandem mass spectrometry of π-expanded triphenylamine and N-heterotriangulene scaffolds: Radical cation versus silver(I) adduct","authors":"Marina Kinzelmann,&nbsp;Nina Fröhlich,&nbsp;Alexander Vogel,&nbsp;Milan Kivala,&nbsp;Thomas Drewello","doi":"10.1002/jms.5079","DOIUrl":"10.1002/jms.5079","url":null,"abstract":"<p>Triphenylamine (TPA) and <i>N</i>-heterotriangulene (<i>N</i>-HTA) scaffolds with up to three oligophenyl extensions are investigated by electrospray ionization (tandem) mass spectrometry (ESI-[MS/]MS). Due to their low oxidation potentials, all molecules readily form radical cations in the electrospray process. The energy-resolved collision-induced dissociation behaviour of the molecular ions is contrasted to that of the silver(I) adducts. Complexation with Ag(I) leads to the expected [1:1] and [2:1] complexes (MAg⁺ and M₂Ag⁺); however, even [1:2] complexes (MAg₂²⁺) can be detected for molecules with two and three large π-expansions to allow stabilization of two charges. The TPA scaffolds decompose only at high collision energies through the loss of peripheral <i>tert</i>-butyl groups. A general mechanism for this is proposed commencing with a methyl loss and followed by the release of <i>iso</i>butene and butyl radical moieties. The <i>N</i>-HTA-based scaffolds are considerably less stable and molecular ions fragment at low collision energies. This is caused by the facile loss of methyl radicals from the dimethylmethylene-bridged triangulene core. In contrast, complexation with Ag⁺ leads to a dramatic stabilization. Most interestingly, dissociation eventually proceeds via the loss of neutral AgCH₃, which is indicative of strong bidentate, tweezer-like bonding of Ag⁺ to the molecules.</p>","PeriodicalId":16178,"journal":{"name":"Journal of Mass Spectrometry","volume":null,"pages":null},"PeriodicalIF":1.9,"publicationDate":"2024-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jms.5079","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141916946","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}