Biochimica et biophysica acta. Biomembranes最新文献

{"title":"Evaluation of aquaporin Z water permeability in bilayers using droplet interface systems with internal-pressure–defined membrane tension","authors":"Misuzu Ueki ,&nbsp;Takahisa Maki ,&nbsp;Masayuki Iwamoto","doi":"10.1016/j.bbamem.2025.184425","DOIUrl":"10.1016/j.bbamem.2025.184425","url":null,"abstract":"<div><div>Cell membranes regulate water flow to maintain homeostasis, cell volume, and osmotic balance. Aquaporins (AQPs) enable selective water transport, making precise permeability measurements essential for understanding their function. The current methods have limitations, including high resource demands and poor control over membrane properties like bilayer tension. In this study, the droplet interface bilayer (DIB) system was used to measure aquaporin water channel activity. Unlike conventional water permeability assays, this method uniquely quantifies lipid bilayer tension by determining droplet internal pressure. This pressure-determined DIB (PDIB) method was used to investigate the water permeability of a lipid bilayer reconstituted with <em>Escherichia coli</em> aquaporin Z (AqpZ). Water permeability increased in an AqpZ concentration-dependent manner at bilayer tensions of 2.2–3.0 mN/m and was inhibited by mercury (IC₅₀, 340 μM). Fluorescence microscopy was performed to visualize and quantify AqpZ molecules, thereby allowing us to derive an approximate estimate of the unitary water permeability. Although this study established the PDIB method and demonstrated its applicability to AqpZ, this technique may also facilitate future investigations on the effects of lipid bilayer tension on aquaporin function and the fundamental mechanisms of water transport across biological membranes.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184425"},"PeriodicalIF":2.8,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144115070","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Interactions of hinokitiol with fungal membrane lipids in model systems","authors":"Beata Wyżga ,&nbsp;Magdalena Skóra ,&nbsp;Karolina Olechowska ,&nbsp;Katarzyna Hąc-Wydro","doi":"10.1016/j.bbamem.2025.184423","DOIUrl":"10.1016/j.bbamem.2025.184423","url":null,"abstract":"<div><div>Hinokitiol (β-thujaplicin) is a naturally occurring substance of antimicrobial properties, which can be used e.g. as a cosmetic preservative. In this work the influence of hinokitiol on the monolayers and bilayers formed from fungal membrane lipids (1-palmitoyl-2-oleoyl-<em>sn</em>-glycero-3-phosphoethanolamine – POPE; 1-palmitoyl-2-oleoyl-<em>sn</em>-glycero-3-phosphocholine – POPC and ergosterol) was investigated. These studies aimed to investigate the effect of hinokitiol on fungal membranes, being indicated as a target for this compound. In this context, the affinity of hinokitiol for ergosterol-containing membranes was of particular interest. The in vitro antifungal activity of hinokitiol was also determined. The results showed that hinokitiol is active against the <em>Candida</em> species tested and exhibits stronger antifungal than antibacterial activity. Moreover, hinokitiol alters the properties of model membranes and the observed effects correlated with ergosterol content in the system. Namely, the higher the ergosterol content, the greater the fluidizing and destabilising effect of hinokitiol and its removal from the model. Moreover, hinokitiol is not able to penetrate into ergosterol membranes; instead, causes strong destabilization of the film and dragging the monolayer material into the subphase. Thus, hinokitiol changes properties of model membrane by the exclusion of the molecules from the interface. The results evidenced differences in the interactions of hinokitiol with ergosterol vs phospholipids, and the interactions of hinokitiol with the membrane depend on the presence and levels of ergosterol. Thus, ergosterol can be a molecular target for this compound. Moreover, the presence of ergosterol in fungal membranes and its lack in bacteria membranes may explain stronger antifungal vs antibacterial effect of hinokitiol.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184423"},"PeriodicalIF":2.8,"publicationDate":"2025-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143916398","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of glucosylation for the vertical movement of cholesterol in bilayer membranes","authors":"Shinya Hanashima ,&nbsp;Takafumi Asahina ,&nbsp;Raymond Malabed ,&nbsp;Katsuaki Sasaki ,&nbsp;Michio Murata","doi":"10.1016/j.bbamem.2025.184422","DOIUrl":"10.1016/j.bbamem.2025.184422","url":null,"abstract":"<div><div>Cholesterol (Chol) in mammalian cell membranes facilitates the assembly of dynamic membrane domains that are involved in vital biological processes through lateral and transbilayer movements in the membranes. In the cell membranes, Chol undergoes glucose transglycosylation to produce cholesteryl-β-<span>d</span>-glucoside (ChoGlc). ChoGlc is involved in neurodegenerative diseases and accumulates in lysosomal storage disorders. However, the effects of glucosylation on membrane properties of Chol remain unclear. We investigated the membrane interaction of ChoGlc and its subsequent translocation between leaflets using fluorescent probes, such as 4-trimethylammoniumphenyl)-6-phenyl-1,3,5-hexatriene (TMA-DPH) and the newly synthesized 7-nitro-2,1,3-benzoxadiazole-labeled ChoGlc (NBD-ChoGlc) in dioleoylphosphatidylcholine (DOPC) membranes. The fluorescence of TMA-DPH, which selectively reported the order of the outer leaflet of the bilayer, indicated that ChoGlc added to the external solution, was mostly incorporated into the membranes and increased the DOPC membrane ordering. Furthermore, the anisotropy values reached a level similar to that of the ChoGlc-preloaded symmetric vesicle within approximately 5 min owing to the rapid distribution of ChoGlc in both leaflets. This was further confirmed by the selective fluorescence quenching of NBD-ChoGlc in the outer leaflet through irreversible quenching by dithionite. The similarity of the fluorescence decay curves of NBD-ChoGlc and NBD-Chol indicated that the glucosylation had little impact on the flip-flops of Chol in the DOPC bilayers. Our data demonstrates that some of the important membrane properties of Chol, such as fast flip-flop between leaflets and increased membrane order, were mostly maintained in ChoGlc despite hydrophilic glucose modification.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184422"},"PeriodicalIF":2.8,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143918419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Elucidating the interactions of endocannabinoid-like neurotransmitters, N-acyltaurines and bovine serum albumin: Spectroscopic and computational approaches","authors":"Martin Luther John ,&nbsp;Sivaramakrishna Akella ,&nbsp;Ravi Kanth Kamlekar","doi":"10.1016/j.bbamem.2025.184421","DOIUrl":"10.1016/j.bbamem.2025.184421","url":null,"abstract":"<div><div><em>N</em>-Acyltaurines (NATs) are endogenous neurotransmitters, structurally similar to endocannabinoids, and have anti-inflammatory and anti-proliferative effects. In response to NATs, TRP channels, TRPV1, TRPV4 and the peptide hormone, GLP-1 are activated. Serum albumin proteins act as transporters for a variety of substances in blood plasma (i.e., hormones, fatty acids, bilirubin, ions, and medications). Due to the structural closeness of Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA), a study into NAT-BSA interactions is crucial. To study interactions of NATs (<em>n</em> = 10–18) with BSA, spectroscopic and computational techniques were used. From the steady-state fluorescence measurements, observed binding constants are in the range of 1.57 × 10⁵ M⁻¹ to 2.85 × 10⁵ M⁻¹. Due to the binding of NATs, the fluorescence of BSA is quenched (∼24.77 %). The negative enthalpy and entropy change and Gibbs free energy values, obtained from van't Hoff plot indicate that the interactions between NATs and BSA are spontaneous and primarily driven by hydrogen bonding. Competitive site-binding assays with warfarin and ibuprofen show that NATs bind to both the drug-binding sites in BSA concurrently. The CD spectroscopic and FT-IR analysis indicates relatively marginal changes in the secondary structure of BSA. Molecular docking analyses are done to identify binding locations and molecular-level interactions. The negative free energy values indicate that NATs have a positive binding relationship with BSA. These findings are congruent with the findings of site-binding studies, which reveal that NATs have a higher proclivity for interacting with sites I and II at the same time.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184421"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143844050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of osmolytes on the conformational stability of Aβ(25–35): A circular dichroism analysis","authors":"Angelo Santoro ,&nbsp;Michela Buonocore ,&nbsp;Anna Maria D'Ursi","doi":"10.1016/j.bbamem.2025.184420","DOIUrl":"10.1016/j.bbamem.2025.184420","url":null,"abstract":"<div><div>Alzheimer's (AD) is a neurodegenerative disease characterized by the onset and progression of mental decline. AD aetiopathogenesis is still questioned; however, according to one of the most accredited hypotheses, the accumulation of amyloid plaques formed by aggregated Aβ peptides is the primary cause of neuronal function loss. Accordingly, hundreds of molecules have been screened for their possible action to prevent or destroy amyloid aggregates. Following this track, osmolytes, naturally occurring small molecules produced by several organisms in response to external stressors, were recently evaluated as modulators of Aβ aggregation. In this study, we examined the conformational stability of Aβ(25–35) when exposed to the osmolytes acetylcholine (ACh), succinylcholine (SCh), and betaine (Bet). Aβ(25–35) is the shortest fragment known for replicating the aggregation process seen in Aβ peptides. By collecting circular dichroism (CD) spectra in water and different membrane-mimicking systems, we investigated the potential of the mentioned osmolytes to stabilize the soluble conformations of Aβ(25–35) and preserve them from denaturing conditions. Our data suggest that Bet is a promising small molecule that can safeguard the soluble form of Aβ peptide and is effective in counteracting environmental conditions by favoring the amyloid aggregation associated with pathology progression.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184420"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787660","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Structural analysis of the NK-lysin-derived peptide NK-2 upon interaction with bacterial membrane mimetics consisting of phosphatidylethanolamine and phosphatidylglycerol” [BBA – Biomembr. 1866 (2024) 184267]","authors":"Jörg Andrä ,&nbsp;Christopher Aisenbrey ,&nbsp;U.S. Sudheendra ,&nbsp;Marc Prudhon ,&nbsp;Gerald Brezesinski ,&nbsp;Evgeniy S. Salnikov ,&nbsp;Claudia Zschech ,&nbsp;Regine Willumeit-Römer ,&nbsp;Matthias Leippe ,&nbsp;Thomas Gutsmann ,&nbsp;Burkhard Bechinger","doi":"10.1016/j.bbamem.2025.184416","DOIUrl":"10.1016/j.bbamem.2025.184416","url":null,"abstract":"","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184416"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143381577","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Long-chain cationic gemini surfactants as drug retention adjuvant on liposomes. A methodological approach with atorvastatin","authors":"Yago Radziunas-Salinas ,&nbsp;Vicente Domínguez-Arca ,&nbsp;Alberto Pardo ,&nbsp;Adriana Cambón ,&nbsp;Pablo Taboada ,&nbsp;Gerardo Prieto","doi":"10.1016/j.bbamem.2025.184419","DOIUrl":"10.1016/j.bbamem.2025.184419","url":null,"abstract":"<div><div>This study delves into the development and characterization of dipalmitoyl phosphatidylcholine (DPPC) liposomes incorporated with gemini surfactant (tetradecamethylene-1,14 bis(dimethyl tetradecyl ammonium bromide); 14-14-14) and atorvastatin, aimed at enhancing drug delivery efficiency for cardiovascular diseases. The integration of gemini surfactants into liposomes is investigated for its potential to improve atorvastatin encapsulation and retention, addressing the drug's poor water solubility and the limitations of conventional liposomal systems. Through a combination of dynamic light scattering (DLS), differential scanning calorimetry (DSC), and molecular dynamics (MD) simulations, the study reveals that the presence of gemini surfactants significantly reduces liposome size and polydispersity, indicative of a more uniform and potentially unilamellar structure. DSC analysis highlights a decrease in transition temperatures and an alteration in transition symmetry, suggesting enhanced stability and a favourable drug release profile at physiological temperatures. MD simulations provide insight into the internalization mechanism of gemini surfactants and atorvastatin within the liposomal bilayer, demonstrating their mutual incorporation facilitated by polar interactions. Spectrophotometry-based retention studies further confirmed that liposomes containing gemini surfactants exhibit superior atorvastatin retention capabilities, nearly doubling the encapsulation efficiency compared to conventional liposomes. This research highlights the promising role of gemini surfactant-incorporated liposomes as an efficient drug delivery platform for cardiovascular therapeutics, offering insights into the molecular interactions and structural dynamics underlying their enhanced performance.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184419"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787602","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Replacement of phenyl substituents at phosphorus by hexyl ones in 2-(2-hydroxyaryl)vinylphosphonium salts can tune the nature of the induced proton transport through lipid membranes","authors":"Tatyana I. Rokitskaya ,&nbsp;Ljudmila S. Khailova ,&nbsp;Anna G. Strelnik ,&nbsp;Elena A. Kotova ,&nbsp;Vladimir F. Mironov ,&nbsp;Dmitry A. Tatarinov ,&nbsp;Yuri N. Antonenko","doi":"10.1016/j.bbamem.2025.184417","DOIUrl":"10.1016/j.bbamem.2025.184417","url":null,"abstract":"<div><div>2-(2-hydroxyaryl)vinylphosphonium salts are zwitterionic protonophores previously shown to induce proton transport across lipid membranes via cyclic deprotonation and protonation of the hydroxyl group. Here, we examine the impact of the kind of substituents at phosphorus on the protonophoric activity of these compounds. In particular, replacement of all the three phenyl groups at the phosphorus atom of the 2-(2-hydroxyaryl)vinyl(triphenyl)phosphonium salt (<strong>2HVPPh</strong>_{<strong>3</strong>}) by hexyl chains (<strong>2HVPHex</strong>_{<strong>3</strong>}) led to a tremendous increase in electric current induced by the phosphonium salt across planar bilayer lipid membranes (BLM). Remarkably, the BLM conductance quadratically increased with increasing <strong>2HVPHex</strong>_{<strong>3</strong>} concentration, whereas a linear concentration dependence of the BLM current was observed for <strong>2HVPPh</strong>_{<strong>3</strong>}, <strong>2HVPHexPh</strong>_{<strong>2</strong>} ((hexyl)diphenyl) and <strong>2HVPHex</strong>_{<strong>2</strong>}<strong>Ph</strong> ((dihexyl)phenyl), i.e., in the presence of at least one phenyl substituent at the phosphorus atom. Proton selectivity of the <strong>2HVPHex</strong>_{<strong>3</strong>}-induced electric current was close to perfect in membranes formed of diphytanylphosphatidylcholine with the decreased dipole potential, but rather low in membranes formed of the usual synthetic lipid – diphytanoylphosphatidylcholine. We hypothesize that the proton transport across BLM is carried out by <strong>2HVPHex</strong>_{<strong>3</strong>} dimers. By contrast, the uncoupling activity of <strong>2HVPHex</strong>_{<strong>3</strong>} in isolated rat liver mitochondria was observed at similar concentrations, as found for the compounds with phenyl substituents, thereby indicating that dimers do not play a key role in the uncoupling process. At the same time, the rate of <strong>2HVPHex</strong>_{<strong>3</strong>}-induced mitochondrial swelling under the deenergized conditions in potassium acetate medium, reflecting the protonophoric activity of the compound in mitochondria, significantly exceeded that for other compounds.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 3","pages":"Article 184417"},"PeriodicalIF":2.8,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143453902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lipopolysaccharide supramolecular organization regulates the activation of coagulation factor XII","authors":"André L. Lira ,&nbsp;Ting Liu ,&nbsp;Joseph E. Aslan ,&nbsp;Cristina Puy ,&nbsp;Owen J.T. McCarty","doi":"10.1016/j.bbamem.2025.184415","DOIUrl":"10.1016/j.bbamem.2025.184415","url":null,"abstract":"<div><div>Lipopolysaccharides (LPS) are key bacterial membrane components that activate coagulation factor XII (FXII), establishing a critical link between bacterial infections, blood coagulation, and inflammation. This study investigates how the supramolecular organization of LPS—monomers, micelles, and bilayers—affects FXII activation. We demonstrate that LPS micelles uniquely activate FXII to its enzymatic form (FXIIa), while monomeric LPS modulates FXIIa activity without direct activation, and bilayer-form LPS does not induce FXII activation. The addition of calcium ions (Ca²⁺) promoted the formation of bilayers by binding to the negatively charged phosphate groups of LPS, reducing electrostatic repulsion and stabilizing LPS aggregates, potentially leading to a shift in their net charge. These findings highlight the pivotal role of LPS supramolecular structure in modulating FXII activity, providing mechanistic insights into the interplay between bacterial components and the coagulation cascade.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 3","pages":"Article 184415"},"PeriodicalIF":2.8,"publicationDate":"2025-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143349958","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lock and key: Quest to find the most compatible membrane mimetic for studying membrane proteins in native environment","authors":"Rahul Yadav ,&nbsp;Debarghya Pratim Gupta ,&nbsp;Chandan Singh","doi":"10.1016/j.bbamem.2025.184414","DOIUrl":"10.1016/j.bbamem.2025.184414","url":null,"abstract":"<div><div>Membrane proteins play crucial roles in cellular signal transduction, molecule transport, host-pathogen interactions, and metabolic processes. However, mutations, changes in membrane properties, and environmental factors can lead to loss of protein function. This results in impaired ligand binding and misfolded structures that prevent proteins from adopting their native conformation. Many membrane proteins are also therapeutic targets in various diseases, where drugs can either restore or inhibit their specific functions. Understanding membrane protein structure and function is vital for advancing cell biology and physiology. Experimental studies often involve extracting proteins from their native environments and reconstituting them in membrane mimetics like detergents, bicelles, amphipols, nanodiscs, and liposomes. These mimetics replicate aspects of native membranes, aiding in the study of protein behavior outside living cells. Scientists continuously explore new, more native-like membrane mimetics to improve experimental accuracy. This dynamic field involves evaluating the advantages and disadvantages of different mimetics and optimizing the reconstitution process to better mimic natural conditions.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 3","pages":"Article 184414"},"PeriodicalIF":2.8,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143363538","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}