Journal of the American Society for Mass Spectrometry最新文献

{"title":"Molecular Dynamics of Neurotensin and Lysozyme Soft-Landing on Gold: Influence of the Molecular Projectile Velocity, Incidence Angle and Temperature.","authors":"Samuel Bertolini, Arnaud Delcorte","doi":"10.1021/jasms.5c00174","DOIUrl":"https://doi.org/10.1021/jasms.5c00174","url":null,"abstract":"<p><p>Employing large argon cluster ion beams, the iBEAM technique has exhibited aptitude in transferring large intact biomolecules from a target to a collector surface in the vacuum, e.g., lysozyme and glucose oxidase, while preserving their bioactivity. Our molecular dynamics (MD) simulations described the desorption of intact lysozymes, glucose oxidase, and even lysozyme clusters comprising up to five units, thereby suggesting the potential soft desorption of heavy biomolecules and their molecular clusters. In turn, assuming their soft desorption, the present contribution models the landing of a single neurotensin cluster containing 5 neurotensin molecules or one lysozyme molecule onto a gold substrate using reactive MD. The parameter space, including incidence angle, collision velocity, and cluster/protein temperature, is systematically explored. Our simulations show that fragmentation increases with the rise of the velocity, collision angle toward the normal, and temperature. Also, after the collision, the backscattering phenomenon is predominantly influenced by varying the collision velocity but is less affected by the collision angle and temperature. Nonetheless, all molecular projectile parameters play a role in shaping the landing process on gold.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145273304","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":"LCMS/MS-Based Mining of the Peptaibiome: A Discovery of New Peptaibols.","authors":"Nisha Sharma, Poonam Choudhary, Priya Kumari, Mohd Murtaza, Vidushi Abrol, Rohit Singh, Sudha Shankar, Andrew J Wiemer, Manoj Kushwaha, Sundeep Jaglan","doi":"10.1021/jasms.5c00324","DOIUrl":"https://doi.org/10.1021/jasms.5c00324","url":null,"abstract":"<p><p>In this study, we employed liquid chromatography-tandem mass spectrometry (LC-MS/MS) to perform chemo-profiling on four fungal species: three Trichoderma species─two strains of <i>Trichoderma asperellum</i> (S3-3 and S3-1) and one <i>Trichoderma longibrachiatum</i> (FS-46)─and one species from the <i>Tolypocladium</i> genus, <i>Tolypocladium inflatum</i> (MTCC-3538). Our analysis identified 78 peptaibols featuring α-aminoisobutyric acid (Aib). Among these, we discovered both cyclic and linear Peptaibols and lipopeptaibols with Aib, ranging in putative molecular weights from 1033.4 to 1953.6 g/mol, corresponding to peptide lengths of 10-20 amino acids. In total, 78 peptaibols, including lipopeptaibols, were identified through LC-MS/MS. Of these, 43 were recognized as new peptaibols based on mass fragmentation patterns and sequence data from the MS/MS analysis. Our findings suggest that LC-MS/MS-based large-scale studies of the peptaibiome will enable the discovery of novel peptaibols and provide a valuable reference for understanding fragmentation patterns of peptaibols, cyclic peptaibols, and lipopeptaibols. Moreover, LC-MS/MS allows rapid identification of peptaibiotics at low concentrations directly in extracts, offering a potential quality control method for selecting beneficial Trichoderma strains for crop protection, while their fragmentation patterns and plausible sequences can guide synthetic design.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145257024","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":"UV-Vis Action Spectroscopy Reveals Structures of DNA Codon Trinucleotide Cation Radicals.","authors":"Frantisek Tureček, Shu R Huang, Yue Liu","doi":"10.1021/jasms.5c00266","DOIUrl":"https://doi.org/10.1021/jasms.5c00266","url":null,"abstract":"&lt;p&gt;&lt;p&gt;We report a comprehensive spectroscopic study of gas-phase cation radicals and dication radicals derived from DNA trinucleotide codons AAA, AAC, AAT, ATA, and TAA that was augmented by computational analysis of protomer and conformer structures, energies, excited states, and vibronic spectra for AAA, AAC, and AAT cation radicals and AAA and AAC dication radicals. Multiply charged noncovalent complex ions of codons with dibenzo-18-crown-6 ether (DBCE) were generated by electrospray protonation, selected by mass, and used for electron transfer dissociation to cleanly generate codon cation radicals, dication radicals, and doubly reduced ions upon DBCE elimination. Complexes of AAA and AAC formed both doubly and triply charged ions that upon gas-phase reduction and loss of DBCE yielded the respective stable hydrogen-rich cation radicals (AAA + 2H)&lt;sup&gt;+•&lt;/sup&gt; and (AAC + 2H)&lt;sup&gt;+•&lt;/sup&gt; and dication radicals (AAA + 3H)&lt;sup&gt;2+•&lt;/sup&gt; and (AAC + 3H)&lt;sup&gt;2+•&lt;/sup&gt;. The AAT, ATA, and TAA complexes formed doubly charged ions that were used to generate the respective (AAT + 2H)&lt;sup&gt;+•&lt;/sup&gt;, (ATA + 2H)&lt;sup&gt;+•&lt;/sup&gt;, and (TAA + 2H)&lt;sup&gt;+•&lt;/sup&gt; cation radicals. UV-vis photodissociation in the 210-700 nm region was employed to acquire action spectra that characterized valence-electron excitations in the ions. Ion structures were assigned by matching the action spectra with vibronic absorption spectra that were calculated by time-dependent density functional theory for multiple isomers. (AAA + 2H)&lt;sup&gt;+•&lt;/sup&gt; was found to assume a zwitterionic structure with protonated 5'- and 3'-adenine rings, a negative phosphate, and the radical residing at the middle adenine. In contrast, upon formation the (AAA + 3H)&lt;sup&gt;2+•&lt;/sup&gt; dication radical underwent exothermic hydrogen migration to C8 at the 5'-adenine. The different course of hydrogen atom migration was related to the different recombination energies of the dications and trications, and explained by Rice-Ramsperger-Kassel-Marcus theory calculations of rate constants that showed a substantial rate decrease by collisional cooling of the (AAA + 2H)&lt;sup&gt;+•&lt;/sup&gt; isomerization. (AAT + 2H)&lt;sup&gt;+•&lt;/sup&gt; ions that were produced by electron transfer underwent hydrogen atom migrations, forming dihydrothymine radicals and adenine cation radicals, as indicated by the action spectra. Single electron reduction of (AAC + 2H)&lt;sup&gt;2+&lt;/sup&gt; and (AAC + 3H)&lt;sup&gt;3+&lt;/sup&gt; resulted in hydrogen atom migrations between the nucleobases in the cation radicals and dication radicals. Upon formation, the (AAC + 2H)&lt;sup&gt;+•&lt;/sup&gt; cation radicals were found to undergo hydrogen migrations between the adenine rings, forming C8-dihydroadenine radicals, whereas cytosine radicals were indicated only weakly by the action spectra. Action and vibronic spectra of the (AAC + 3H)&lt;sup&gt;2+•&lt;/sup&gt; dication radicals indicated that the ions underwent exothermic isomerizations by hydrogen atom migrations, forming N3,C8-dihydroadenine cation radicals with","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145237644","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":"Targeted Metabolomics of <i>Tityus</i> Scorpion Venoms: Unveiling Small-Molecule Components.","authors":"Nathalia Baptista Dias, Bibiana Monson de Souza, Geovanny Barroso, Javier Ortiz Leiva, Gabriela Mendonça Paula, Hipócrates M Chalkidis, Valquíria Abrão Coronado Dorce, Osmar Malaspina, Mario Sergio Palma","doi":"10.1021/jasms.5c00238","DOIUrl":"https://doi.org/10.1021/jasms.5c00238","url":null,"abstract":"<p><p>Scorpion venoms consist of proteins, peptides, and various low molecular weight (LMW) organic compounds, which act as toxins. Despite their potential significance, these compounds in scorpion venoms have been little investigated and their full range has not been well characterized. In this work, a targeted metabolomic approach was used in combination with an HPLC-QTOF-MS methodology to create a library of 55 LMW standard compounds, for the analysis of venoms from three <i>Tityus</i> species scorpions. This strategy enabled reliable identification of 45 compounds, including 20 amino acids, 4 organic acids, 12 biogenic amines, 6 nitrogenated bases and derivatives, 2 β-carboline-derived alkaloids, and 1 amphetamine. Most of the compounds identified were neurotransmitters and/or neurotoxins, while others can act as homeostasis disruptors or affect the diffusion of venom through the bodies of victims. Therefore, the LMW organic compounds in scorpion venoms play roles in the killing or paralyzing of prey, as well as in defense against large predators.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145243578","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":"Performance Evaluation of Constant Field and Traveling Wave-Based Structures for Lossless Ion Manipulations Devices Coupled to Mass Spectrometry.","authors":"Christopher P Harrilal, Isaac K Attah, Pearl Kwantwi-Barima, Ruwan Kurulugama, Yehia M Ibrahim","doi":"10.1021/jasms.5c00273","DOIUrl":"https://doi.org/10.1021/jasms.5c00273","url":null,"abstract":"<p><p>The performances of three prototype structures for lossless ion manipulations IMS mass spectrometer (SLIM IMS-MS) are evaluated. The instrument was constructed by replacing the drift tube of an Agilent 6560 with either traveling wave (TW) or constant field (CF) based SLIM modules of nearly identical length. The TW-SLIM module contains a 79.4 cm straight path and a 10 m serpentine path. The evaluation of these systems enabled the direct determination of performance differences associated with the drift tube replacement by the SLIM devices. The evaluation included comparing the resolution, resolving power, transmitted mass range, and collisional cross-section (CCS) accuracy relative to its drift tube counterpart for each device/path. Results indicated that the 79.4 cm CF-SLIM displayed comparable performance to the drift tube while the 79.4 cm TW-SLIM path provided ∼25% higher resolution and resolving powers (<i>R</i>_p) (<i>R</i>_p = 67-90 for a range of singly charged analyte ions) compared to the drift tube. The 10 m path showed an increase of up to 300%. Synchronizing the introduction of ions from the ion funnel trap with the traveling waveform enabled the mitigation of mass discrimination during ion transfer into the TW-SLIM module, resulting in an <i>m</i>/<i>z</i> distribution similar to that of the drift tube. A comparison of CCS obtained with the drift tube and TW/CF-SLIM IMS shows good overall agreement (∼±1.5%) for most of the molecular classes investigated. The results presented here provide a normalized comparison between the separation methods, highlighting the advantages and areas for improvement in SLIM-based ion mobility devices.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145231037","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":"Proteoform Characterization of HIV-1 Broadly Neutralizing Antibody PGT 121.414.LS Product Through Middle-Up and Bottom-Up Proteomics for Clinical Support.","authors":"Connor E Gould, Qing Ma, Raymond Cha, Valerie A Frerichs, Alan E Friedman, Robin DiFrancesco, Gene D Morse, Troy D Wood","doi":"10.1021/jasms.5c00198","DOIUrl":"https://doi.org/10.1021/jasms.5c00198","url":null,"abstract":"<p><p>Broadly neutralizing antibody (bNAb) therapies are under development for the prevention and treatment of HIV-1 infection as an alternative to conventional antiretroviral therapy because of their potential for sustained passive immunotherapy. Currently, bNAbs targeting the HIV-1 viral envelope proteins are included in research protocols to evaluate their role in preventing transmission and in combination antiviral regimens to achieve viral suppression. While quantification of bNAbs is of clinical importance, validation of the structural fidelity of therapeutic antibodies is also an important consideration to assess the clinical efficacy. Here, we applied middle-up and bottom-up proteomics workflows for the quality assurance of the primary structure of the HIV-1 bNAb PGT 121.414.LS product. Middle-up and bottom-up proteomics workflows were performed using liquid chromatography coupled to an Orbitrap mass spectrometer. Middle-up analysis of the crystallizable fragment (Fc/2), light chain (Lc), and fragment denaturation (Fd, N-terminal fragment of the heavy chain) regions of PGT 121.414.LS was performed by using IdeS digestion, which revealed proteoform heterogeneity. To complement the middle-up approach, a bottom-up workflow combining trypsin and chymotrypsin digests was performed for detailed glycoform mapping and annotation. The bottom-up results indicated that Lc contained an additional N-terminal Ser residue. For the Fc, two abundant and two lower-abundance glycoforms of the heavy chain were detected that correspond to Asn-312 (Asn-297 in the consensus heavy chain sequence of IgG). For Fd, bottom-up analysis revealed eight sialylated glycoforms and five nonsialylated glycoforms at Asn-124 of the heavy chain. The results emphasize bNAb heterogeneity, which should be considered in affinity binding studies.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145211311","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":"ASMS from an Editor-in-Chief's Perspective: Welcoming an Industrial Associate Editor to the JASMS Team.","authors":"Jenny Brodbelt","doi":"10.1021/jasms.5c00291","DOIUrl":"https://doi.org/10.1021/jasms.5c00291","url":null,"abstract":"","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145211321","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":"Improving the Quadrupole to Ion Mobility Region in a Digital Quadrupole/Ion Mobility/Orbitrap Mass Spectrometer.","authors":"Robert L Schrader, Gordon A Anderson, Kacie A Evans, David H Russell","doi":"10.1021/jasms.5c00142","DOIUrl":"https://doi.org/10.1021/jasms.5c00142","url":null,"abstract":"<p><p>A quadrupole/drift tube ion mobility/Orbitrap instrument requires pumping from atmosphere to 10^-5 Torr in the quadrupole analyzer region, back to 1 Torr for the drift tube, and a return to 10^-5 Torr for the Orbitrap high vacuum region. The Orbitrap high vacuum region contains the transfer multipole, C-trap, and HCD cell. Insufficient pumping between the drift tube and quadrupole leads to helium in the quadrupole analyzer chamber which compromises performance. Additional vacuum regions were added between the drift tube and the analyzer chamber to maintain the analyzer pressure below 5.5 × 10^-5 Torr with the drift tube pressurized to 1.5 Torr of He. In this configuration, the isolation of a single charge state of C-reactive protein (<i>m</i>/<i>z</i> 5,000) was demonstrated. Fourier transform ion mobility spectra were acquired with the quadrupole in full scan mode and in the isolation mode. Ion optic voltages were optimized for both helium and nitrogen bath gases in the drift tube so that minimal ion heating was observed entering the drift tube. These instrument modifications enable improved ion transfer efficiency, allowing for better ion isolation by the digital quadrupole ion mobility separation of large protein complexes, as illustrated by the 23+ and 24+ charge states of C-reactive protein.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145211326","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":"An Integrated Strategy for Rapid Profiling of Depsipeptides by High-Performance Liquid Chromatography Coupled to Quadrupole Time-of-Flight Mass Spectrometry: <i>Bombyx batryticatus</i> as an Example.","authors":"Huijie Sun, Yang Li, Yunhua Feng, Kaicheng Xie, Jinyi Sui, Ting Wu, Hongliang Zhou, Guoliang Dai, Chengyao Ma, Jiandong Zou, Meijuan Xu","doi":"10.1021/jasms.5c00259","DOIUrl":"https://doi.org/10.1021/jasms.5c00259","url":null,"abstract":"<p><p>Depsipeptides, a structurally diverse class of nonribosomal peptides with broad bioactivities, present significant challenges for systematic characterization due to their complex fragmentation patterns in mass spectrometry (MS). This study aims to develop a generic three-step strategy based on high-performance liquid chromatography quadrupole time-of-flight mass spectrometry (HPLC-Q-TOF/MS) to facilitate the rapid screening and identification of both linear and cyclic depsipeptides. The workflow is defined by three sequential, logic-driven steps: (1) filtering potential depsipeptide precursors via diagnostic and adduct ions along with depsipeptide classification; (2) identifying the structural residues by monitoring diagnostic product ions and neutral losses; and (3) sequencing the peptide backbone through comprehensive analysis of MS/MS spectra. To validate the strategy's universality, it was applied to the analysis of depsipeptides in a complex biological matrix (extracts of <i>Bombyx batryticatus</i>). A total of 62 depsipeptides (encompassing octa-, hexa-, tetra-, and didepsipeptides, with both cyclic and linear topologies) were identified or tentatively characterized, including 34 potential novel analogs. Notably, the strategy successfully distinguished 10 methionine-containing depsipeptides with subtle redox modifications (native methionine, methionine sulfoxide, methionine sulfone), demonstrating its ability to resolve structurally similar derivatives. This three-step strategy offers a simple, rapid, and robust tool for comprehensive depsipeptide profiling. Its application to complex matrices highlights the strong potential for extending to other biological samples, advancing systematic analysis of depsipeptide families in natural products and biological systems.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145211272","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":"Applications of DESI and DART Mass Spectrometry in Forensic Science.","authors":"Nathália Dos S Conceição, Alan R Pereira, Daniel S Trancoso, João Victor M de Almeida, Nicole Souza do Carmo, Nayara A Dos Santos, Hildegardo S França, Marc Yves Chalom, Wanderson Romão","doi":"10.1021/jasms.5c00175","DOIUrl":"https://doi.org/10.1021/jasms.5c00175","url":null,"abstract":"<p><p>Ambient Mass Spectrometry (AMS) has revolutionized forensic analysis by enabling rapid and direct detection of chemical compounds on complex surfaces with minimal or no sample preparation. Among AMS techniques, desorption electrospray ionization (DESI) and direct analysis in real time (DART) mass spectrometry have emerged as powerful analytical tools due to their speed, sensitivity, and versatility. This review examines the major applications of DESI and DART in forensic science, including the detection of explosives, gunshot residue, illicit drugs, inks, biological fluids, and latent fingerprints. The principles of each technique are briefly discussed, followed by a comparative analysis of their advantages, limitations, and performances in various forensic scenarios. Recent developments, practical considerations for implementation, and future perspectives are also addressed, highlighting the growing impact of DESI and DART in real-time forensic investigations and evidence processing.</p>","PeriodicalId":672,"journal":{"name":"Journal of the American Society for Mass Spectrometry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145205306","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}