Journal of the American Society for Mass Spectrometry最新文献

{"title":"Advancing O-Glycosylation Analysis of Fc-Fusion Proteins at the Domain Level by HILIC-MS with Supercharging.","authors":"Xiaojuan Li, Hongxia Wang, Ekaterina G Deyanova","doi":"10.1021/jasms.6c00242","DOIUrl":"https://doi.org/10.1021/jasms.6c00242","url":null,"abstract":"<p><p>Fragment crystallizable (Fc)-fusion proteins are formed by the fusion of functional peptides or receptor extracellular domains (ECDs) with Fc. They are normally very heterogeneous with multiple N- and O-glycosylation sites and a high level of sialylation. Characterization of O-glycosylation in Fc-fusion proteins is important for understanding their biological significance and for monitoring process consistency during drug development. However, due to the heterogeneity, close localization, and especially low ionization efficiency of O-glycans, it is challenging to achieve the overall O-glycosylation profile at the protein level. In this study, a supercharging reagent, m-nitrobenzyl alcohol (m-NBA), was applied to mobile phases for hydrophilic interaction liquid chromatography-mass spectrometry (HILIC-MS) analysis of two Fc-fusion proteins at the domain level. The addition of m-NBA mitigated MS signal suppression caused by TFA in mobile phases and enabled the characterization of the overall O-glycosylation profiles of ECDs. While de-N-glycosylation of Fc resulted in only a slight increase in MS signal intensity, the average MS signal intensity of the top three ECD-derived O-glycoforms increased by approximately 11.4- to 13.0-fold and 6.9- to 10.8-fold for these Fc-fusion proteins with and without terminal sialic acid, respectively. This observation indicates that m-NBA facilitates increased MS signal intensity for glycosylated proteins, with a pronounced effect on sialylated species. In addition, the enhanced MS signal intensity of major released N-glycans achieved through supercharging enabled their identification without the need for sample separation, derivatization, and enrichment. Overall, this HILIC-MS method combined with supercharging provides a promising approach for domain-level characterization of O-glycans and simultaneous analysis of released N-glycan without derivatization.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.9,"publicationDate":"2026-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149163624","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":"Unifying Passive Air Sampling with Paper Spray Ionization Mass Spectrometry for the Detection of Third-Hand Cigarette Smoke","authors":"Bo-Cheng Ke,&nbsp;Noor Hidayat Abu Bakar,&nbsp;Pawel L. Urban","doi":"10.1021/jasms.6c00271","DOIUrl":"https://doi.org/10.1021/jasms.6c00271","url":null,"abstract":"<p>To mitigate human exposure to air pollutants amid theincreasingchemicalization of daily life, simple and rapid monitoring methodsare required. As individuals spend a significant portion of theirtime indoors, indoor air quality has become a critical factor affectinghuman health and is influenced by a wide range of indoor and outdoorpollution sources. The sorption and desorption of indoor air pollutantson solid surfaces (the so-called <em>sink effect</em>) cangradually increase pollutant concentrations and lead to changes inindoor air quality. In particular, third-hand smoke (THS), a persistentform of indoor pollution, poses potential health risks through inhalation,dermal contact, and ingestion. Air sampling and analysis can be tediousand costly. Here, we present a very simple method that unifies passivesampling of THS onto paper and subsequent analysis by paper sprayionization (PSI) mass spectrometry (MS). Mass spectrometric resultsrevealed the presence of nicotine, a major constituent of tobaccosmoke, in THS samples collected using a custom-built passive sampler,which was further confirmed by MS/MS analysis. The applicability ofthis approach was further extended to a forensic context by detectingnicotine on book pages, which were previously exposed to cigarettesmoke, using filter papers as sampling media. Overall, passive airsampling onto paper─combined with PSI-MS─provides asimple, cost-effective, and time-efficient way for indoor air qualitymonitoring and forensic analysis.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2534–2541"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149093603","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":"MALDI MSI Workflow for Pharmaceutical Tablets: Toward a Reproducible Strategy for High-Resolution Imaging","authors":"Athina Lisgara,&nbsp;Alvaro Santos-Neto,&nbsp;Georgia Charkoftaki,&nbsp;Reza Aalizadeh,&nbsp;Michelle Raikes,&nbsp;Scott Pennino,&nbsp;John A. Smoliga,&nbsp;Michael Becker,&nbsp;Vladimir V. Papov, Jr.,&nbsp;Nina Gonnella,&nbsp;Vasilis Vasiliou","doi":"10.1021/jasms.6c00161","DOIUrl":"https://doi.org/10.1021/jasms.6c00161","url":null,"abstract":"<p>Mass spectrometry imaging (MSI) can complement liquidchromatography–massspectrometry (LC-MS), the gold standard for impurity assessment, byenabling spatial visualization of active pharmaceutical ingredients(APIs), byproducts, and excipients in solid formulations. With newadvances in matrix-assisted laser desorption/ionization (MALDI) MSI,critical factors such as ablated spot size, raster speed, and standardizedtablet surface preparation still need to be properly addressed. Thisstudy presents an innovative sample holder and sample preparationprotocol enabling reproducible up to 10-μm step size acquisitionfor MSI analysis of tablets. The workflow was validated by embeddingseveral commercial tablets containing various APIs in blocks withepoxy resin, then transversally cut them to expose their surfaces.Following this, the tablet surfaces were trimmed using a cryostatand subsequently polished with lapping diamond films to achieve flatand even surfaces. The tablets were then placed in a custom metalholder for MALDI-trapped ion mobility spectrometry (TIMS)-MSI analysisusing a timsTOF fleX. The optimized protocol provides high-qualitysample preparation and avoids loss of laser focus, enabling high-throughputanalysis with high sensitivity for tablet imaging. This robustnesswas essential for spatial resolution measurements using the Smartbeam3D, where precise initial focusing is required to preserve data qualityacross imaging areas. Consistent high signal sensitivity was achievedfor single pixels in 10 mg cetirizine or 20 mg famotidine tabletsand digoxin fragments were detected in a 0.25 mg/130 mg tablet. Thisapproach provides an important tool for pharmaceutical developmentby enabling reliable, high-resolution spatial analysis of active ingredientsand impurities in solid dosage forms. Collision cross section (CCS)values from reference standards and tablets, as well as MS/MS datawere used for confident identification. LC-MS-based workflows remainessential for quantitative analysis of impurity assessment, whileinfrared spectroscopy (IR) and nuclear magnetic resonance (NMR) cansupport formulation level characterization. MALDI-TIMS-MSI complementsthese approaches by adding direct spatial localization of APIs andAPI-related molecular features within the tablet matrix.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2341–2351"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149093608","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":"A Liquid Chromatography-Mass Spectrometry Method to Quantify Total Coenzyme A Concentration and Isotopic Labeling","authors":"Amelia L. Taylor,&nbsp;Nathaniel W. Snyder,&nbsp;Caroline R. Bartman","doi":"10.1021/jasms.6c00206","DOIUrl":"https://doi.org/10.1021/jasms.6c00206","url":null,"abstract":"<p>Coenzyme A is an essential cofactor synthesized frompantothenate,which carries activated acyl groups in cellular metabolic reactions.Coenzyme A participates in catabolism of carbohydrates, fats, andamino acids; biosynthesis of fatty acids, cholesterol, and heme; andprotein modification, including acetylation and 4-phosphopantetheinylation.Despite CoA’s critical functions, the regulation of CoA levelsand the rate of CoA synthesis in different cell types and diseasestates are not well understood. Acyl-CoA species are challenging tomeasure due to instability, poor ionization, and the wide range ofbiochemical properties conferred by different acyl chain lengths;moreover, most current methods cannot measure CoA isotopic labeling,required to quantify the CoA synthesis rate or to measure concentrationusing isotope-labeled internal standards. Here, we describe a methodto quantify the concentration and isotopic labeling of total CoA,defined as the sum of CoASH plus all acyl-CoA species. Acyl-CoA speciesare hydrolyzed using sodium hydroxide to remove acyl chains; then,CoA is derivatized with <em>N</em>-ethylmaleimide (NEM). Followingprotein precipitation and solid-phase extraction, samples are analyzedby liquid chromatography-mass spectrometry. This method is linearin a wide range that captures mouse tissue CoA levels, with accuracywithin 15% error and precision below 15% relative standard deviationfor standards and tissue samples. We applied this method to measuretotal CoA concentration in five mouse tissues and the total CoA synthesisrate in mouse liver via infusion of ¹³C–¹⁵N-pantothenate. Overall, this method offers a tractable approachto measure total CoA concentration and synthesis rate in health anddisease.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2453–2462"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149100839","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":"Differentiation of Cotton Fabrics Using Stable Isotope Ratio Mass Spectrometry","authors":"Jason D. Eckmann,&nbsp;Douglas J. Beussman","doi":"10.1021/jasms.6c00162","DOIUrl":"https://doi.org/10.1021/jasms.6c00162","url":null,"abstract":"<p>White cotton fibers are of specialimportance in forensics dueto bleached cotton’s ubiquity in the clothing industry. Whilethese fibers are often difficult to distinguish using conventionalchemical techniques, stable isotope ratio mass spectrometry has provena useful tool for their analysis. Our goal was to investigate thepotential for applying this technique to the differentiation of t-shirtsand other cotton products. Analysis was performed using an elementalanalyzer, a high-temperature conversion/elemental analyzer, and acontinuous flow isotope ratio mass spectrometer. Cotton samples ofvarious manufacturing origins were analyzed to investigate the homogeneityand differentiability of the samples. Additionally, fibers of samplesoriginating from the same source were studied. Differences betweensewing thread and cloth in clothing samples were also analyzed. Differentiabilitywas determined using ANOVA tests, and visualization was achieved usingthree-dimensional trivariate plot analysis. Each individual cottonsample was found to be largely homogeneous, but samples from differentsources were distinguishable. Sewing thread and cloth fibers werealso found to be differentiable. Based on this pilot study, stableisotope ratio mass spectrometry shows promise as a tool for the analysisof cotton fibers, especially when multiple isotopes are used to discriminatebetween samples.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2352–2356"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149124831","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":"Where Do Proteomics People Come from?","authors":"Benjamin C. Orsburn","doi":"10.1021/jasms.6c00268","DOIUrl":"https://doi.org/10.1021/jasms.6c00268","url":null,"abstract":"<p>Thefield of proteomics is one of the fastest-growingscientificdisciplines in the world today. Beginning in 2020, ambitious marketpredictions anticipated proteomics to more than double in market sizein 4–6 years and to even surpass the well-established genomicsciences industry in 8–12 years. While the market is stillgrowing, it has not come close to matching the initial projections.To better understand the root cause of this, the author has collectedfield surveys and direct interviews of over 200 scientists activelyinvolved in proteomics research today. While ultimately incomplete,it is worth noting that over 68% of respondents received their technicaltraining in proteomics during either their doctoral or postdoctoraltraining. In stark contrast, only 4.3% of students obtained trainingduring their undergraduate education. Given the 5.7-to-9.4-year averagecycle for traditional doctoral and postdoctoral training in the lifesciences, it appears the limiting factor in growing the proteomicsfield may be linked directly to current practices in training a qualifiedworkforce.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2511–2514"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149124928","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":"Plasma-Assisted Functionalization of Hydrocarbons for Enhanced Mass Spectrometric Detection","authors":"Muhammad Mujahid Ali,&nbsp;Manish Jana,&nbsp;Myles Q. Edwards,&nbsp;Shiva Ataei,&nbsp;R. Graham Cooks","doi":"10.1021/jasms.6c00269","DOIUrl":"https://doi.org/10.1021/jasms.6c00269","url":null,"abstract":"<p>The detection andstructural analysis of hydrocarbons by mass spectrometry(MS) are challenging because of poor ionization. Here, we report aplasma-based strategy that selectively converts nonpolar hydrocarbonsto derivatives that are mass spectrometry-friendly by controlled oxygenand nitrogen insertion reactions. A subatmospheric pressure plasmafacilitates stable discharges under mild conditions, allowing theformation of ketones, unsaturated ketones, and imines without structuralfragmentation or extensive oxidation. The reaction pathways can betuned by adjusting the carrier gas and sample introduction mode, allowingcontrolled switching between simple oxidation, dehydrogenation, andnitrogen insertion. Mass spectrometric analysis reveals well-definedmolecular ions that show characteristic fragmentation behavior intandem MS, facilitating improved detection and structural interpretationacross linear, branched, cyclic, and aromatic hydrocarbons. Furthermore,a scalable method has been developed to achieve preparative levelsof modified samples for NMR analysis, and this confirmed ketone formationas the dominant oxygen-insertion pathway. Overall, this work demonstratesa simple and versatile plasma-based approach for enhancing the detectionand structural characterization of otherwise challenging hydrocarbonspecies.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2515–2524"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149124860","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":"Resonant RF Circuit Enables Ion Containment and m/z-Dependent Axial Ejection for Corrected Time-of-Flight Discrimination","authors":"Nathan K. Kaiser,&nbsp;Gordon A. Anderson,&nbsp;William R. Kew,&nbsp;Christopher L. Hendrickson,&nbsp;Chad R. Weisbrod","doi":"10.1021/jasms.6c00246","DOIUrl":"https://doi.org/10.1021/jasms.6c00246","url":null,"abstract":"<p>Time-of-flight <em>m</em>/<em>z</em> discriminationlimits the effective analytical <em>m</em>/<em>z</em> range for Fourier transform ion cyclotron resonance (FT-ICR) massspectrometry because optimal ion arrival time at the ICR cell varieswith <em>m</em>/<em>z</em>^1/2. Previously,an auxiliary RF waveform that allowed sequential <em>m</em>/<em>z</em>-dependent axial ejection from an external ionaccumulation multipole resulted in mitigation of time-of-flight <em>m</em>/<em>z</em> discrimination, which improved iontransfer across a decade in the <em>m</em>/<em>z</em> range 200–2000. Here, a resonant RF axial ejection systembased upon the same principle is implemented to further expand the <em>m</em>/<em>z</em> range that can be observed in a singlemass spectrum. This new RF ejection system was installed without anychange to the internal vacuum components. The RF ejection system hasbeen significantly simplified over the initial implementation andinstalled and verified on several FT-ICR mass spectrometers in a multilabcollaboration.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2623–2627"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149093569","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":"ICARION: A Modular Framework for Ion Trajectory Simulation in Electric Fields and Neutral Gas Environments","authors":"Christoph Schaefer,&nbsp;Juraj Jašík,&nbsp;Patrik Španěl","doi":"10.1021/jasms.6c00235","DOIUrl":"https://doi.org/10.1021/jasms.6c00235","url":null,"abstract":"<p>Ion transport in electric fields and neutral gases underliestheoperation of ion mobility spectrometers, mass spectrometers, and coupledIMS-MS instruments. Numerical modeling of such systems requires consistenttreatment of field-driven motion, stochastic ion-neutral collisions,and reactions across different pressure and field regimes. Many IMS-MSinstruments operate in transitional regimes, requiring explicit particle-basedtreatment of collisions. Here, we present ICARION (Ion Collision AndReaction IntegratiON), an open-source, modular, particle-based simulationframework for reproducible simulations of ion transport, collisions,and reactions. ICARION is intended for mechanistic studies of iondynamics, exploration of new concepts in IMS, MS, and related techniques,and rapid and reproducible screening of operating parameters and geometriesfor instrument development and optimization. Its modular architecturecombines various selectable field, collision, and reaction modelswith structured configuration and data processing. Multiple instrumentdomains with different electric fields, geometries, and environmentalconditions can be seamlessly combined in a single simulation of coupledIMS-MS instruments. This work validates ICARION rather than introducingnew physical models. Validation includes collisional thermalization,bimolecular reaction kinetics, ion transport in homogeneous electricfields validated with established tools, and coupled multidomain simulations.Across these cases, ICARION reproduces the expected behavior of theselected physical models and enables continuous simulations acrossdomains differing by orders of magnitude in pressure and field timescales. While externally generated field maps can be integrated asneeded, a planned internal field solver will enable the calculationof electric fields directly from the user-defined electrode configurations.The modular architecture also facilitates the integration of additionalphysical models.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2483–2496"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149093639","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":"A Streamlined One-Pot Extraction Method Enables High-Sensitivity Top-Down Proteomic Characterization of Phospholamban from Biopsy-Scale Cardiac Tissue","authors":"Isabella R. Clemmer,&nbsp;Holden T. Rogers,&nbsp;Mallory C. Wilson,&nbsp;Zhan Gao,&nbsp;Hsin-Ju Chan,&nbsp;Zachery R. Gregorich,&nbsp;Farhan Raza,&nbsp;Ying Ge","doi":"10.1021/jasms.6c00309","DOIUrl":"https://doi.org/10.1021/jasms.6c00309","url":null,"abstract":"<p>Top-downproteomics (TDP) enables comprehensive characterizationof intact proteoforms, but the analysis of membrane proteoforms remainschallenging because of their hydrophobicity and relatively low abundance.To address these challenges, we previously developed Azo, a photocleavablesurfactant that enables efficient solubilization and top-down analysisof membrane proteins. Subsequently, we established an Azo-enabledTDP method permitting the comprehensive characterization of phospholamban(PLN), a transmembrane protein that plays crucial roles in calciumhandling, directly from cardiac tissue. However, the original workflowrequired at least 10 mg of human cardiac tissue, making it unsuitablefor biopsy-scale and other sample-limited studies. Herein, we developeda streamlined Azo-enabled one-pot extraction strategy for high-sensitivitytop-down analysis of PLN that reduces the required tissue input to1 mg while preserving analytical performance. Using online liquidchromatography–tandem mass spectrometry, we achieved highlyreproducible detection, quantification, and post-translational modificationlocalization of endogenous PLN proteoforms from 1 mg of human cardiactissue. Notably, the streamlined strategy reduced the tissue requiredfor PLN protein extraction 10-fold while retaining the same capacityfor comprehensive characterization in the one-pot extraction. Collectively,these results establish a practical strategy for TDP of PLN proteoformsfrom biopsy-scale and other sample-limited myocardial specimens.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":"37 10","pages":"2273–2280"},"PeriodicalIF":2.9,"publicationDate":"2026-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149093649","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}