Biochimica et biophysica acta. Biomembranes最新文献

{"title":"The impact of vitamin E and its acetate derivative on lipid dynamics of unsaturated membrane systems.","authors":"Maksymilian Dziura, Iain McKenzie, Kevin L Weiss, Brandon Nusser, Honghai Zhang, Hugh M O'Neill, Piotr A Zolnierczuk, Eugene Mamontov, Drew Marquardt","doi":"10.1016/j.bbamem.2026.184580","DOIUrl":"https://doi.org/10.1016/j.bbamem.2026.184580","url":null,"abstract":"<p><p>While α-tocopherol (αToc) is fundamentally recognized as a membrane-resident antioxidant, its synthetic derivative, α-tocopheryl acetate (αTocAc), has recently gained notoriety as a primary diluent in illicit vaping products associated with E-cigarette or Vaping Use-Associated Lung Injury (EVALI). The pathophysiology of EVALI has been linked to the disruption of pulmonary surfactant (PS) membranes, yet the specific impact on lipid dynamics and mechanical stability remains poorly defined. This study employs avoided level crossing muon spin resonance (ALC-μSR), quasielastic neutron backscattering (QENS), and neutron spin echo (NSE) to quantify the impacts of αToc and αTocAc on 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) and multicomponent PS mimic systems at a physiological temperature of 37 °C. ALC-μSR measurements reveal that αToc restricts local acyl chain dynamics, causing a 50% increase in the motionally averaged dipolar coupling that reduces the tail wobbling cone half-angle (θ_C). On a mesoscopic scale, QENS demonstrates that low concentrations (2-5 mol%) of αToc and αTocAc suppresses lateral lipid diffusivity (D_lat) in pure POPC from a baseline of 0.51×10^-10m²/s down to a minimum of 0.35×10^-10m²/s, following a non-monotonic trend that recovers near 10 mol%. Concurrently, NSE reveals a pronounced concentration-dependent stiffening of the fluid POPC bilayer, where αTocAc increases the bending modulus (κ) from a baseline of 17.9±0.7k_BT up to ≈31k_BT at 10 mol%, outstiffening the impact of its natural counterpart. Conversely, the unsaturated fraction of a complex PS mimic maintains a stable dynamic profile (D_lat≈0.35×10^-10m²/s), pointing to possible linactant compartmentalization at phase boundaries or clustering. Together, these multiscale findings establish a lipid-centric, biophysical mechanism for EVALI, where αTocAc restrict lateral lipid mobility and over-stiffen the fluid-phase reservoirs of the lung, fundamentally impeding the critical compression-expansion respreading mechanics of pulmonary surfactant required for normal respiration.</p>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":" ","pages":"184580"},"PeriodicalIF":2.4,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206466","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":"In vitro and in silico studies of the membrane interactions of mollusk-derived antimicrobial peptides Pom-1 and Pom-2.","authors":"Brandt Bertrand, A J Otero-Gonzalez, Carlos Munoz-Garay","doi":"10.1016/j.bbamem.2026.184583","DOIUrl":"https://doi.org/10.1016/j.bbamem.2026.184583","url":null,"abstract":"<p><p>Pom-1 and Pom-2 are antimicrobial peptides natively produced by the fresh-water snail Pomacea poeyana. They selectively kill bacteria and yeasts, but present no cytotoxic effects for mammalian cells, and their mode of action is still unclear. Liposome calcein leakage experiments were used to measure permeability effects of both peptides, while Laurdan generalized polarization (GP) was used to determine the effect of the AMPs on apparent membrane fluidity. Only Pom-1 induced dye leakage, with the greatest activity in the bacterial model, following modest activity in the fungal model, and no activity towards the mammalian membrane. Likewise, the greatest effect on membrane fluidity induced by Pom-1 was observed in the bacterial model, with slight changes registered with the fungal model. The effect of the peptide was dosis-dependent. The intrinsic tryptophan fluorescence spectroscopy of Pom-1 indicated that, at a minimum, the hydrophobic N-terminal end of the peptide inserted into all three membranes. Molecular dynamics simulations corroborated the in vitro observations, as Pom-2 did not interact with or perturb membrane properties. Although Pom-1 showed greater free binging energy with the bacterial model, it inserted to a greater depth into the fungal membrane, but without significantly modifying membrane properties. The different capabilities of Pom-1 and Pom-2 to interact with the different bilayers were mainly due to biochemical properties of the peptides such as net charge a neutral pH, hydrophobicity, Bowman index, among others. Pom-1´s secondary structure was stable throughout the simulations, while Pom-2 tended to denature over time. The in-silico analyses suggested that peptide aggregation negatively impacted membrane peptide interaction and subsequent insertion. Conclusively, we present strong evidence that the plasma membrane is the molecular target of Pom-1; The Pom-2 target remains unknown.</p>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":" ","pages":"184583"},"PeriodicalIF":2.4,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206482","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":"Probing bacteriophage-induced membrane perturbation in Aeromonas salmonicida subsp. salmonicida by in-cell solid-state NMR.","authors":"Rana Moussaoui, Stéphane Beauclercq, Valérie E Paquet, Alexandre A Arnold, Steve J Charette, Isabelle Marcotte","doi":"10.1016/j.bbamem.2026.184582","DOIUrl":"https://doi.org/10.1016/j.bbamem.2026.184582","url":null,"abstract":"<p><p>Aeromonas salmonicida subsp. salmonicida is a major bacterial pathogen of salmonids in aquaculture, and bacteriophage therapy could provide an alternative to antibiotics for its control. Bacteriophage infection of this Gram-negative bacterium begins at the cell surface and involves interactions with outer membrane components including lipopolysaccharides and surface structures such as the A-layer. Although these interactions influence phage adsorption, their impact on bacterial membrane organization remains poorly understood. Here, we investigated membrane dynamics in three strains differing in envelope architecture and phage sensitivity: AS-R3 (A-layer-positive, phage-sensitive), AS-R5 (A-layer-negative, phage-sensitive), and BIM93 (A-layer-negative, phage-insensitive). We used in vivo²H solid-state nuclear magnetic resonance combined with phospholipid and fatty acid analyses. Exogenous perdeuterated palmitic acid enabled efficient membrane labelling in intact bacteria without significantly altering the overall lipid composition. While all strains shared similar phospholipid classes, BIM93 displayed a higher proportion of saturated fatty acids and increased membrane order than AS-R3 and AS-R5. Upon exposure to phage SW69-9, membrane order decreased markedly in the sensitive strains, with a pronounced loss of viability in AS-R5. In contrast, BIM93 maintained membrane organization and high viability, whereas AS-R3 showed an intermediate response with significant membrane perturbation despite limited cell lysis. These results indicate that phage-induced membrane perturbations depend on both phage sensitivity and bacterial envelope architecture. More broadly, they suggest that changes in membrane organization during phage exposure are influenced by surface-associated bacterial structures. This study highlights the role of bacterial surface structures and membrane physical properties in shaping phage-host interactions.</p>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":" ","pages":"184582"},"PeriodicalIF":2.4,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149206507","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":"Interaction of elastin-derived peptides with model lipid membranes.","authors":"Manon Ragouilliaux, Jean-Marc Crowet, Frank Wien, Magali Deleu, Laurent Debelle, Nicolas Belloy","doi":"10.1016/j.bbamem.2026.184578","DOIUrl":"https://doi.org/10.1016/j.bbamem.2026.184578","url":null,"abstract":"<p><p>Elastin-derived peptides (EDPs), generated during elastin fragmentation in aging and pathological conditions, are widely recognized for their biological activity through interactions with cell-surface receptors. However, despite their hydrophobic character and proximity to membrane-associated receptors, their capacity to directly interact with lipid bilayers has remained largely unexplored. In this study, we investigated the membrane-binding properties of representative elastin hexa and nonapeptides using a combination of molecular dynamics simulations, potential of mean force calculations, and synchrotron radiation circular dichroism spectroscopy. Our results reveal that the hexapeptide displays minimal membrane interactions while nonapeptides bearing the XGXPGXGXG consensus motif exhibit significant and dynamic membrane association. Cholesterol markedly reduces membrane affinity and membrane interaction stabilizes β-turn conformations, particularly type II turns. Together, these findings demonstrate that certain elastin nonapeptides are capable of direct lipid-bilayer interactions, unveiling a previously underappreciated physicochemical dimension of EDP activity. By providing a receptor-independent route through which EDPs could influence cell behavior wherever they accumulate, this membrane-binding capability may contribute to their biological effects and offers a new perspective on elastin fragmentation in aging and disease.</p>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":" ","pages":"184578"},"PeriodicalIF":2.4,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149191097","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":"Corrigendum to \"Topological mapping establishes signal peptide-independent cytoplasmic membrane insertion of bacterial MATE family efflux protein EmmdR\" [BBA - Biomembranes, 1868 (2026), 184566].","authors":"Hitkarsh Kushwaha, Jiban Mishra, Harapriya Mohapatra","doi":"10.1016/j.bbamem.2026.184571","DOIUrl":"https://doi.org/10.1016/j.bbamem.2026.184571","url":null,"abstract":"","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":" ","pages":"184571"},"PeriodicalIF":2.4,"publicationDate":"2026-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148849679","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":"Blood coagulation protein binds to Ca2+-induced phosphatidylserine nanodomains as revealed by atomic force microscopy","authors":"Jie Cheng ,&nbsp;Junhong Lü ,&nbsp;Xueling Li","doi":"10.1016/j.bbamem.2026.184500","DOIUrl":"10.1016/j.bbamem.2026.184500","url":null,"abstract":"<div><div>The interaction between coagulation factor VIII (FVIII) and phospholipid membranes is a critical aspect of the blood clotting process. While it is known that FVIII binds to negatively charged phospholipids, the role of calcium ions (Ca²⁺) in this process remains an area of ongoing research. This study investigated the dynamic effects of Ca²⁺ on FVIII binding to phospholipid membranes, in particular how Ca²⁺-induced nanodomain formation affects this interaction. Using in situ atomic force microscopy (AFM) imaging, we observed the morphological and structural changes of supported lipid bilayers (DPPC/DOPS and DOPC/DPPS systems) in response to Ca²⁺. The results showed that Ca²⁺ not only alters the membrane lipid structure, but also promotes the formation of nanodomain in the phosphatidylserine (PS)-enriched regions. In the presence of Ca²⁺, FVIII bound preferentially to PS nanodomains with height differences of about 0.8 nm compared to adjacent membrane regions, and the binding process was further facilitated by Ca²⁺-induced reorganization of the lipid phases over time scales of 40–230 min. These findings provided new insights into the molecular mechanisms governing the interaction of FVIII with phospholipid membranes and underlined the crucial role of Ca²⁺ in supporting the functional activity of coagulation protein.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1868 2","pages":"Article 184500"},"PeriodicalIF":2.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146002972","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":"Acylation of the RTX toxin MbxA stimulates host membrane disruption through a specific interaction with cholesterol","authors":"Feby Mariam Chacko ,&nbsp;Sarah Michelle Ganz ,&nbsp;Anne Pfitzer-Bilsing ,&nbsp;Sebastian Hänsch ,&nbsp;Philipp Westhoff ,&nbsp;Stefanie Weidtkamp-Peters ,&nbsp;Sander H.J. Smits ,&nbsp;Marten Exterkate ,&nbsp;Lutz Schmitt","doi":"10.1016/j.bbamem.2025.184487","DOIUrl":"10.1016/j.bbamem.2025.184487","url":null,"abstract":"<div><div>RTX toxins (Repeat in ToXins) are pore-forming toxins secreted by gram-negative bacteria. They are known for their ability to disrupt host cell membranes, among which various human cells. The acylation of specific lysine residues in these toxins is crucial for their hemolytic activity, but the precise mechanisms underlying this enhancement remain unclear. By comparing the lytic activities of acylated MbxA and its non-acylated form, we explored the role of acylation in the pore-forming behavior of this RTX toxin. Our findings demonstrate that acylation specific interactions of MbxA with cholesterol promote membrane disruption, both <em>in vitro</em> and in living cells. More specifically, acylation is not necessary for initial membrane binding, but markedly enhances pore formation. Overall, our results provide detailed insights into the molecular determinants that regulate MbxA toxin activity. We highlight a complex interplay between lipid composition (sterols), acylation, and membrane disruption, thereby advancing our general understanding of RTX toxin pathogenesis.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1868 2","pages":"Article 184487"},"PeriodicalIF":2.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145628387","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":"Reverse micelles produce hydroxyapatite nanoparticles as more efficient gene delivery carriers than regular micelles","authors":"Vuk Uskoković","doi":"10.1016/j.bbamem.2026.184506","DOIUrl":"10.1016/j.bbamem.2026.184506","url":null,"abstract":"<div><div>Hydroxyapatite (HAp) is an effective inorganic gene delivery carrier due to its ability to transport genetic cargo across cell membranes, protect it from proteolysis, and enable escape from late endosomes via pH-controlled dissolution. However, its transfection efficiency remains lower than that of viral agents, prompting studies of hybrids with cationic molecules or phases to enhance the gene delivery performance. This study reports on the synthesis of HAp in regular and reverse micellar regions of a ternary microemulsion system composed of cetyltrimethylammonium bromide (CTAB), 1-hexanol and water. Spectroscopic characterization revealed that CTAB headgroups adopted more ordered supramolecular conformations in reverse micelles compared to regular ones. Similarly, water within reverse micelles exhibited more homogeneity and unexpected freedom, creating favorable entropic conditions for chemical reactions. CTAB showed strong electrostatic affinity for DNA and bound more effectively to HAp synthesized within the confined nanoscale environment of reverse micelles than to HAp produced in the aqueous continuum surrounding regular micelles. Also, reverse micelles produced narrowly dispersed, rod-shaped HAp nanoparticles, unlike the larger, macroporous particles formed in regular micelles. Both of these effects predisposed HAp from reverse micelles to exhibit a higher transfection efficiency in K7M2 osteosarcoma cells than its regular micelle counterpart. Despite these positive outcomes, HAp could only partially mitigate the cytotoxic effects of CTAB. Therefore, further exploration of advanced synthesis methods, biocompatible surfactants or strategies to preserve the synergy between HAp, CTAB and DNA while reducing CTAB toxicity is essential for enhancing the gene delivery performance of reverse micellar HAp.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1868 2","pages":"Article 184506"},"PeriodicalIF":2.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146043557","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 ice recrystallization inhibition on hydrogen bonding interactions and membrane leakage of liposomes","authors":"Dejia Liu ,&nbsp;Harriëtte Oldenhof ,&nbsp;Harald Sieme ,&nbsp;Willem F. Wolkers","doi":"10.1016/j.bbamem.2026.184502","DOIUrl":"10.1016/j.bbamem.2026.184502","url":null,"abstract":"<div><div>In this study, effects of ice recrystallization on membrane stability of liposomes were investigated using liposomes encapsulating a fluorescent dye. Membrane leakage was studied after freezing and storage at varying temperatures in solutions supplemented with polyvinyl alcohol (PVA), polyethylene glycol (PEG), dimethyl sulfoxide (DMSO) and combinations thereof. Leakage studies were corroborated with studies on ice crystal growth and hydrogen bonding interactions during holding at temperatures just below the ice melting temperature, i.e., at −10 °C. Cryomicroscopic observations confirmed that PVA exhibits ice recrystallization inhibition activity, whereas PEG did not. Both PVA and PEG reduced freezing-induced liposome leakage, alone and in combination with low DMSO concentrations. Temperature-scanning infrared spectroscopy (FTIR) combined with principal component analysis (PCA) was used as a novel approach to probe differences in hydrogen bonding interactions between frozen buffered saline (PBS) containing PVA and PEG. Score and loading plots show that symmetric hydrogen bonds are predominant with addition of PVA, and that the cluster of principal component data points remain compact during holding under ice recrystallization conditions. By contrast, PBS supplemented with PEG and PBS control solutions are characterized by weak hydrogen bonding interactions and more disperse clusters of principal component data points denoting rearrangements in hydrogen bonding interactions associated with ice crystal growth during holding. In conclusion, beneficial effects of adding PVA or PEG in cryopreservation solutions for liposomes are most evident under suboptimal cryopreservation conditions, e.g., during storage at elevated subzero temperatures, and when low concentrations of DMSO are used.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1868 2","pages":"Article 184502"},"PeriodicalIF":2.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146028343","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":"Biophysical approaches to antimicrobial peptide–membrane characterization","authors":"A. Roldán ,&nbsp;P. Fernández-García ,&nbsp;V. Lladó ,&nbsp;M. Torres ,&nbsp;P.V. Escribá ,&nbsp;M. Salvador-Castell","doi":"10.1016/j.bbamem.2026.184499","DOIUrl":"10.1016/j.bbamem.2026.184499","url":null,"abstract":"<div><div>Antimicrobial peptides (AMPs) represent a current strategy to develop new antibiotics against multi-resistant pathogens. The potential antibiotic activity of AMPs is related to their amphipathic properties and the presence of positively charged residues, which may interact with the negatively charged bacterial membranes. In contrast, they exhibit lower interaction with the eukaryotic, neutrally charged membranes. This is the primary reason AMPs can distinguish between eukaryotic and prokaryotic membranes.</div><div>AMPs are usually modified or designed <em><strong>de novo</strong></em>, and their properties can be changed by inserting specific amino acid residues into their sequence. To assist in the rational design of AMPs, it is helpful to explore the biophysical changes they may induce in target cell membranes. Therefore, bacterial and eukaryotic model lipid membranes have been extensively used for this purpose. Parameters such as selective binding, lipid membrane interactions, membrane packing, permeability, hydration, and restructuring facilitate the exploration of peptide regions of interest. These parameters can be studied using various physicochemical techniques, including differential scanning calorimetry, X-ray diffraction, nuclear magnetic resonance, and fluorescence spectroscopy.</div><div>This review aims to provide a practical guide to the main biophysical techniques used to explore the potential antibiotic activity of AMPs using model membranes, and to examine lipid-peptide interactions in order to define the mechanisms of action of these antimicrobial peptides. These techniques determine whether the peptide interacts specifically with bacterial membranes, the preferred bacterial target of a given AMP, the binding affinities of AMPs, potential pore formation and its geometry, and the impact of these interactions on both bacterial and eukaryotic membranes.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1868 2","pages":"Article 184499"},"PeriodicalIF":2.5,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145987895","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}