BioelectrochemistryPub Date : 2025-01-31DOI: 10.1016/j.bioelechem.2025.108920
Xiaoshuai Peng , Guojian Li , Jiu Zhao , Huatao Liu , Changhua Wu , Zepeng Su , Zhidong Liu , Shuai Fan , Yuanquan Chen , Yanfeng Wu , Wenjie Liu , Huiyong Shen , Guan Zheng
{"title":"Promotion of quiescence and maintenance of function of mesenchymal stem cells on substrates with surface potential","authors":"Xiaoshuai Peng , Guojian Li , Jiu Zhao , Huatao Liu , Changhua Wu , Zepeng Su , Zhidong Liu , Shuai Fan , Yuanquan Chen , Yanfeng Wu , Wenjie Liu , Huiyong Shen , Guan Zheng","doi":"10.1016/j.bioelechem.2025.108920","DOIUrl":"10.1016/j.bioelechem.2025.108920","url":null,"abstract":"<div><div>The widespread use of human mesenchymal stem cells(hMSCs) is impeded by functional loss during prolonged expansion. Although multiple approaches have been attempted to preserve hMSCs stemness, a suitable culture system remains to be modified. The interaction between electrical signals and stem cells is expected to better maintain the function of stem cells. However, it remains unclear whether the surface potential of substrates has the potential to preserve stem cell function during in vitro expansion. In our study, hMSCs cultured on materials with different surface potentials could be induced into a reversible quiescent state, and we demonstrated that quiescent hMSCs could be reactivated and transitioned back into the proliferation cell cycle. hMSCs cultured under appropriate potential displayed superior differentiation and proliferation abilities within the same generation compared to conventional conditions. These findings underscore the importance of surface potential as a critical physical factor regulating hMSCs stemness. Manipulating the surface potential of hMSCs culture substrates holds promise for optimising preservation and culture conditions, thereby enhancing their application in tissue repair and regeneration engineering.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108920"},"PeriodicalIF":4.8,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143154584","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":"Electrochemical and computational studies on the interaction between calf-thymus DNA and skin whitening agent arbutin","authors":"Maryam M.M. Mahdi, Alper Fitoz, Ceren Yıldız, Dilek Eskiköy Bayraktepe, Zehra Yazan","doi":"10.1016/j.bioelechem.2025.108923","DOIUrl":"10.1016/j.bioelechem.2025.108923","url":null,"abstract":"<div><div>The interaction between double-stranded calf thymus DNA (<em>ctDNA</em>) and the skin whitening agent arbutin (<em>AR</em>) examined by applying electrochemical and computational methods for the first time in literature. A single-use pencil graphite electrode via cyclic (<em>CV</em>) and differential pulse voltammetry (<em>DPV</em>) techniques were applied to determine the kinetic and thermodynamic parameters in the absence and presence of <em>ctDNA</em>. To examine the interaction process, oxidation peak currents and potentials of <em>AR</em> were observed prior to the addition of various <em>ctDNA</em> concentrations. The binding constants (<em>K<sub>AR-DNA</sub></em>) and Gibbs free energy (Δ<em>G°</em>) values for the <em>AR-DNA</em> complex were determined as <em>1.82 × 10</em><sup>4</sup> <em>L/mol</em> and <em>−24.30 kJ/mol</em> at 298 K, respectively. Temperature evaluation of the interaction was examined using thermodynamic parameters (Δ<em>H°: −30.30 kJ/mol</em> and Δ<em>S°: −0.00197 kJ/mol</em>) applying the Van’t Hoff equation. The local interaction sites in the molecule structure were determined by applying Fukui functions and second-order perturbation theory in view of potential hydrogen binding centers. The optimized structure of <em>AR</em> was applied with a <em>DNA</em> structure revealing the binding position for <em>AR-DNA</em> complex. Experimental and computational examinations suggested that <em>AR-DNA</em> binds to <em>ctDNA</em> through a minor groove mode via conventional hydrogen bonds, hydrophobic interactions and van der Waals forces.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108923"},"PeriodicalIF":4.8,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143078235","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}
BioelectrochemistryPub Date : 2025-01-30DOI: 10.1016/j.bioelechem.2025.108925
Yuxuan Zang , Bo Cao , Xuemei Yi , Fan Zha , Yanhong Ge , Hong Liu , Yue Yi
{"title":"Enhancing water toxicity determination sensitivity by using TMAO as electron acceptor of inward extracellular electron transfer in electrochemically active bacteria","authors":"Yuxuan Zang , Bo Cao , Xuemei Yi , Fan Zha , Yanhong Ge , Hong Liu , Yue Yi","doi":"10.1016/j.bioelechem.2025.108925","DOIUrl":"10.1016/j.bioelechem.2025.108925","url":null,"abstract":"<div><div>Toxicity determination based on electrochemically active bacteria (EAB) shows great prospects for early warning of sudden water pollution. However, the main bottleneck for practical application is the low sensitivity. Extracellular electron transfer (EET) is a key parameter influencing sensitivity. Our previous research has demonstrated that EAB exhibit higher sensitivity when performing inward EET compared with outward EET. Inward EET relies on electron acceptors, but the effects of electron acceptors on sensitivity remain unclear. In this study, the sensitivity of toxicity determination with different electron acceptors was compared. Results indicated that the choice of electron acceptors significantly changed the sensitivity. When Trimethylamine N-oxide (TMAO) was chosen as the electron acceptor, EAB exhibited the highest sensitivity, with a lower response limit of 0.05 mg/L Cd<sup>2+</sup>. The main reason was that the utilization of TMAO for inward EET increases the membrane permeability of EAB cells, facilitates toxic pollutant penetration, and results in high mortality after toxicity exposure.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108925"},"PeriodicalIF":4.8,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143078257","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}
BioelectrochemistryPub Date : 2025-01-28DOI: 10.1016/j.bioelechem.2025.108921
Himanshu Khandelwal , Sakuntala Mutyala , Minsoo Kim , Da Seul Kong , Jung Rae Kim
{"title":"Whole-cell redox biosensor for triclosan detection: Integrating spectrophotometric and electrochemical detection","authors":"Himanshu Khandelwal , Sakuntala Mutyala , Minsoo Kim , Da Seul Kong , Jung Rae Kim","doi":"10.1016/j.bioelechem.2025.108921","DOIUrl":"10.1016/j.bioelechem.2025.108921","url":null,"abstract":"<div><div>Organic pollutants like bisphenol, acetaminophen, and triclosan, widely used in healthcare products, pose environmental risks and act as endocrine disruptors. These pollutants can alter the intracellular redox balance, making engineered whole-cell redox biosensors valuable for their detection. This study utilized the SoxRS regulatory system in bacteria, which responds to oxidative stress through NADP<sup>+</sup>/NADPH levels by modulating gene expression of SoxS through the SoxS promoter (pSoxS). A plasmid containing SoxR-pSoxS and the LacZ reporter gene was constructed and introduced into <em>E. coli</em> BL21 (ΔLacZ SoxRS+). The LacZ gene enabled dual detection using O-nitrophenyl-β-galactopyranoside (ONPG) for spectrophotometric detection or p-aminophenyl β-D-galactopyranoside (PAPG) for electrochemical detection. The whole-cell pRUSL12 redox biosensor was activated by redox inducers such as pyocyanin and methyl viologen, measurable via β-galactosidase assays. Among pollutants tested, triclosan specifically repressed SoxR:pSoxS::lacZ activity in the presence of pyocyanin or methyl viologen. Optimization identified pyocyanin as the more effective inducer for triclosan detection, with the biosensor capable of detecting triclosan in the 100–400 µg/L range. These redox-based biosensors offer a powerful tool for monitoring metabolic redox changes and identifying specific organic pollutants in the environment.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108921"},"PeriodicalIF":4.8,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143155966","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":"Bidirectional electro-enzymatic reaction of coenzyme F420 using benzyl viologen and F420-dependent sulfite reductase","authors":"Satoshi Furota , Masanori Kaneko , Seiya Tsujimura , Daijiro Takeshita , Yusuke Nakamichi , Kensuke Igarashi , Masaru K. Nobu , Miho Yoshikawa , Kenta Asahina , Chie Fukaya , Toshie Ishitsuka , Kazuma Shimada","doi":"10.1016/j.bioelechem.2025.108922","DOIUrl":"10.1016/j.bioelechem.2025.108922","url":null,"abstract":"<div><div>Coenzyme F<sub>420</sub> is recognized as a crucial electron carrier in methane-generating metabolism but, beyond this, has garnered significant attention for its role in diverse microbial physiologies and relevance in industrial, medical, and environmental applications. However, one limitation of current application of F<sub>420</sub> is the necessity of chemical electron donors for its reduction. In this study, an electrochemical reaction system was designed to facilitate electron transfer between the electrode and F<sub>420</sub> using F<sub>420</sub>-dependent sulfite reductase (Fsr) as the catalyst and benzyl viologen (BV) as the redox mediator. Photometric analysis and cyclic potential scanning demonstrated that the occurrence of bidirectional (reversible) electrochemical oxidation and reduction of F<sub>420</sub> in this system depended on the electrode potential. The formal redox potential of F<sub>420</sub> in this system was −540 mV vs. Ag|AgCl|sat. KCl, which aligned with values previously determined using biochemical assays.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108922"},"PeriodicalIF":4.8,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143072976","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}
BioelectrochemistryPub Date : 2025-01-27DOI: 10.1016/j.bioelechem.2025.108910
Ondrej Hesko , Hana Pivoňková , Lukáš Fojt , Andrew Taylor , Jaromír Kopeček , Karolina Schwarzová-Pecková , Miroslav Fojta
{"title":"Characterization of boron doped diamond electrodes with engineered sp2 carbon content and their application to structure-dependent DNA hybridization","authors":"Ondrej Hesko , Hana Pivoňková , Lukáš Fojt , Andrew Taylor , Jaromír Kopeček , Karolina Schwarzová-Pecková , Miroslav Fojta","doi":"10.1016/j.bioelechem.2025.108910","DOIUrl":"10.1016/j.bioelechem.2025.108910","url":null,"abstract":"<div><div>Boron doped diamond electrodes brought a new potential in bioanalytical chemistry including studies of structure and interactions of nucleic acids. Herein, deposition conditions<!--> <!-->were optimized to produce a set of polycrystalline BDD electrodes with comparable boron concentration in solid phase of (1.8 − 2.1) · 10<sup>21</sup> cm<sup>−3</sup> akin to metallic-type conductivity but with increasing sp<sup>2</sup> <!-->carbon content. Increase of<!--> <!-->[CH<sub>4</sub>]/[H<sub>2</sub>]<!--> <!-->from 0.25 % to 2.0 % during deposition led to an obvious decrease in grain size from <em>ca.</em> <!-->300 nm (BDD<sub>0.25</sub>) to < 100 nm (BDD<sub>2.0</sub>). Adsorption of oligodeoxynucleotides and their structural changes in the presence of K<sup>+</sup> and Li<sup>+</sup> ions were evaluated through enzyme-linked DNA hybridization assay in which oxidizable 1-naphthol was released from its phosphoester<!--> <!-->by<!--> <!-->streptavidin–alkaline phosphatase conjugate upon successful hybridization of the target oligodeoxynucleotide with a biotinylated complementary probe. With increasing sp<sup>2</sup> <!-->carbon content, the hybridization assay showed improved discrimination between a target forming guanine quadruplex (stabilized by K<sup>+</sup> ions), yielding by 40 % – 60 % lower hybridization signal with the complementary probe, compared to the same but unstructured target oligodeoxynucleotide in the presence of Li<sup>+</sup> <!-->ions that don’t stabilize the quadruplex structure. Such behaviour was observed also for commercial BDD electrode with surface roughness < 10 nm.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108910"},"PeriodicalIF":4.8,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143155964","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}
BioelectrochemistryPub Date : 2025-01-27DOI: 10.1016/j.bioelechem.2025.108918
Shi Wang , Jialin Ao , Saiwen Ding , Ting Shu
{"title":"Label-free electrochemical immunosensors based on Cu-Ni metal–organic framework and carbon nanotube composite for carcinoembryonic antigen detection","authors":"Shi Wang , Jialin Ao , Saiwen Ding , Ting Shu","doi":"10.1016/j.bioelechem.2025.108918","DOIUrl":"10.1016/j.bioelechem.2025.108918","url":null,"abstract":"<div><div>Monitoring cancer biomarkers is of great significance in clinical diagnosis. In this work, a label-free MWCNTs-COOH/CuNi-BTC/FTO electrochemical immunosensor was developed to quantitatively detect carcinoembryonic antigen (CEA). The bimetallic CuNi-BTC showed enhanced current than singe Ni-BTC, and the addition of the MWCNTs-COOH increased the conductivity and further amplified the current signal. The electrode was further modified with CEA antigen (Ag) and bovine serum albumin (BSA) was used to block the non-specific binding sites. Using the emplified current signal of CuNi-BTC, CEA was detected by a DPV method through the current change caused by the specific recognition reaction of Ag and Ab. Under optimal conditions, a range of 0.80–140 ng/mL and a detection limit of 0.046 ng/mL for CEA was obtained. This electrochemical immunosensor possessed good selectivity, reproducibility and long-term stability.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"163 ","pages":"Article 108918"},"PeriodicalIF":4.8,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143062731","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}
BioelectrochemistryPub Date : 2025-01-27DOI: 10.1016/j.bioelechem.2025.108919
Wassim El Housseini , François Lapicque , Alain Walcarius , Elisabeth Lojou , Nicolas Rouhier , Mathieu Etienne
{"title":"Ferredoxin NADP+ reductase for NADPH and NADH regeneration in a flow bioelectrochemical reactor","authors":"Wassim El Housseini , François Lapicque , Alain Walcarius , Elisabeth Lojou , Nicolas Rouhier , Mathieu Etienne","doi":"10.1016/j.bioelechem.2025.108919","DOIUrl":"10.1016/j.bioelechem.2025.108919","url":null,"abstract":"<div><div>Ferredoxin-NADP<sup>+</sup> reductase (FNR) is an efficient and selective biocatalyst to continuously regenerate the NADPH cofactor consumed in biomolecular synthesis for the chemical and pharmaceutical sectors. In this work, FNR from <em>Chlamydomonas reinhardtii</em> was applied to electrochemical regeneration of the nicotinamide cofactors, by combining this enzymatic catalyst in a flow reactor with the oxidation of hydrogen, a clean source of electrons and protons. FNR was immobilized on the surface of oxidized multi-walled carbon nanotubes, which allowed maintaining its activity for over six days under high flow rate. Surprisingly, this modified FNR electrode was effective not only in regenerating NADPH but also NADH. The cofactor regeneration was then applied to the NADH-dependent production of lactate from pyruvate, using L-lactate dehydrogenase (LDH) in the presence of low NAD<sup>+</sup> concentration (10 µM). Both FNR and LDH enzymes were immobilized in the bioelectrochemical system that achieved a remarkable total turnover number (TTN) of 10<sup>4</sup> for the nicotinamide cofactor and a faradaic efficiency higher than 80 %.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108919"},"PeriodicalIF":4.8,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143155965","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}
BioelectrochemistryPub Date : 2025-01-26DOI: 10.1016/j.bioelechem.2025.108911
Shaheda Zannah, Damien W.M. Arrigan
{"title":"Exploring the electrochemical behaviour of digestive enzymes at a liquid|liquid micro-interface array","authors":"Shaheda Zannah, Damien W.M. Arrigan","doi":"10.1016/j.bioelechem.2025.108911","DOIUrl":"10.1016/j.bioelechem.2025.108911","url":null,"abstract":"<div><div>Trypsin and pepsin are proteolytic enzymes secreted by the digestive system to digest proteins. Here, we examine the electrochemical behaviour and detection of trypsin and pepsin at a liquid/liquid (L|L) micro-interface array. For both proteins, aqueous phase of 10 mM hydrochloric acid was the only electrolyte solution in which they were electroactive. Neither protein was detected below 30 μM by cyclic voltammetry (CV) but stripping voltammetry following adsorption (AdSV) enabled the detection of sub-micromolar concentrations of both proteins. Although pepsin was electroactive at the micro-interface array in aqueous phase of 10 mM HCl, its behaviour was ill-defined and unsuitable for characterization by CV. It was found that pepsin easily blocked the micro-interfaces, as seen by greatly hampered ion transfer voltammetry of tetrapropylammonium ion (TPrA<sup>+</sup>) whereas trypsin only slightly impeded TPrA<sup>+</sup> transfer. This highlights the dissimilarity between pepsin and trypsin. These results illustrate the rich viability of electrochemistry at L|L micro-interface arrays as a tool to explore the behaviour and detection of biological macromolecules.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108911"},"PeriodicalIF":4.8,"publicationDate":"2025-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143372069","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":"Paper-based electrochemiluminescence telomerase activity detection using hybridization chain reaction and CRISPR/Cas12a dual signal amplification","authors":"Yun Zhang , Liang Gao , Zhe Shi , Qiong Wu , Xiangmin Miao","doi":"10.1016/j.bioelechem.2025.108916","DOIUrl":"10.1016/j.bioelechem.2025.108916","url":null,"abstract":"<div><div>Sensitive telomerase activity detection becomes particularly significance since the important value of it in early cancer diagnosis as a potential biomarker. Herein, we developed a paper-based analytical devices (PADs) for telomerase activity detection, using positively charged Au@luminol nanoparticles ((+)Au@luminol NPs) as electrochemiluminescence (ECL) signal probe coupling with hybridization chain reaction (HCR) and CRISPR/Cas12a dual signal amplification. Firstly, the initial strong ECL signal was obtained based on the electrostatic adsorption of (+)Au@luminol NPs onto the surface of HCR double-stranded hybrid aggregates. In the presence of telomerase, the primer was efficiently elongated with telomeric repeats of (TTAGGG)<sub>n</sub> to release activator DNA and trigger the CRISPR/Cas12a, which can prevent the happen of HCR and the adsorption of (+)Au@luminol NPs through cleaving the capture probe on the electrode surface, such results directly inducing the decrease of the ECL signal that was proportional to telomerase concentration, due to the efficient signal amplification of HCR and CRISPR/Cas12a, a low detection limit of 2.3 cells/mL for telomerase could be detected. Moreover, the sensor realized the effective application for telomerase extracts analysis in human serum samples, making it possess potential application value for telomerase activity assays in cancer diagnostics.</div></div>","PeriodicalId":252,"journal":{"name":"Bioelectrochemistry","volume":"164 ","pages":"Article 108916"},"PeriodicalIF":4.8,"publicationDate":"2025-01-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143155422","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}