Biophysical chemistry最新文献

{"title":"The effect of lipid saturation on the formation of styrene maleic acid lipid nanoparticles","authors":"Emma A. Gordon ,&nbsp;Evelyn A. Okorafor ,&nbsp;Indra D. Sahu ,&nbsp;Kevin M. Burridge ,&nbsp;Muhammad Zeeshan Shah ,&nbsp;Onisha Thapa ,&nbsp;Dominik Konkolewicz ,&nbsp;Gary A. Lorigan","doi":"10.1016/j.bpc.2025.107566","DOIUrl":"10.1016/j.bpc.2025.107566","url":null,"abstract":"<div><div>The ability to use styrene maleic acid (SMA) to solubilize membrane proteins has been of significant interest. The formation of the lipid nanodiscs and extraction of the proteins without the use of detergent allows for the study of these membrane proteins in a more native environment. Traditional mimetic systems, such as micelles, bicelles, and liposomes all have compatibility limitations in their ability to provide a native environment for the protein. Lipid composition plays a significant role in the compatibility of these mimetic systems with membrane proteins. In this study, lipids with varying degrees of saturation are used to assess the efficacy of the SMA polymer in forming styrene maleic acid lipid nanoparticles (SMALPs). Lipids ranging from fully saturated to fully unsaturated are used along with two SMA polymers with various hydrophobic tail lengths. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) are used to characterize the liposomes and SMALPs. Continuous Wave-Electron Paramagnetic Resonance Spectroscopy (CW-EPR) is used to understand the effect of SMA on a spin-labeled membrane protein incorporated in the SMALP system. Results show the dynamic properties of membrane proteins incorporated in SMALPs are dependent on SMA polymer tail length as well as the lipid saturation. Lineshape analysis shows evidence of the hydrophobic tail of the SMA playing a role in how the protein is positioned within the SMALPs.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"331 ","pages":"Article 107566"},"PeriodicalIF":2.2,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145908799","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 surfactin with ether-linked and ester-linked lipid membranes: A molecular dynamics simulation study","authors":"Boggarapu Manasa ,&nbsp;Loknath Patro ,&nbsp;B.L. Bhargava","doi":"10.1016/j.bpc.2025.107567","DOIUrl":"10.1016/j.bpc.2025.107567","url":null,"abstract":"<div><div>Surfactin is a biosurfactant with diverse applications, including antibacterial and antiviral activity, primarily attributed to its ability to destabilize lipid bilayers. Previous studies have focused on ester-linked lipids, where destabilization has been associated with reduced hydration around ester carbonyl groups. Here, we employ molecular dynamics simulations to investigate surfactin’s effect on ether-linked lipids, which lack carbonyl groups and are characteristic of archaeal membranes known for their exceptional stability. We compared tetraether lipids and a diether lipid along with its ester-linked analogue. Among the ether-linked systems, the macrocyclic tetraether lipid showed the strongest response to surfactin insertion, whereas the diether lipid was minimally perturbed. By contrast, the ester-linked analogue underwent significant compression and increased water penetration into the bilayer. These findings reveal that membrane susceptibility to surfactin depends critically on both linkage chemistry and lipid architecture, with ester linkages and tetraether backbones promoting destabilization to a greater extent than diether systems.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107567"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145880388","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":"Modulation of islet amyloid polypeptide induced β-cell toxicity and amyloid formation by serum albumin proteins","authors":"Alexander Zhyvoloup ,&nbsp;Zachary Ridgway ,&nbsp;Ananya Prashanth ,&nbsp;Daniel P. Raleigh","doi":"10.1016/j.bpc.2025.107565","DOIUrl":"10.1016/j.bpc.2025.107565","url":null,"abstract":"<div><div>Human islet amyloid polypeptide (hIAPP, also known as amylin) is a 37-residue neuropancreatic hormone implicated in the progression of type 2 diabetes. hIAPP is soluble and partially structured under physiological conditions, but misfolds to form amyloid deposits in the islets of Langerhans in type 2 diabetes. Along the misfolding pathway, hIAPP forms species that are toxic to pancreatic β-cells, resulting in decreased β-cell function and mass. Serum albumin proteins are a key component of blood plasma and interstitial fluids and are omnipresent in mammalian cell culture media. Immortalized β-cell lines are widely used as model systems for mechanistic studies of hIAPP-induced cytotoxicity and for screening potential inhibitors of hIAPP toxicity. The effects of bovine serum albumin (BSA), human serum albumin (HSA) and fetal bovine serum (FBS) on hIAPP cytotoxicity are examined and the effects of BSA and HSA on hIAPP amyloid formation are explored. The time required for IAPP to form amyloid is lengthened by sub stoichiometric concentrations of BSA and HSA. Cell permeability and cell viability assays with cultured INS 832–13 pancreatic β-cells reveal that BSA, HSA, and FBS reduce hIAPP cytotoxicity. Partial protection against treatment with 40 μM hIAPP is observed for serum albumin concentrations that are only one tenth (=3.75 μM) of the normal amount present in a regular complete cell media containing 10 % FBS. The implications for <em>in vitro</em> assays of hIAPP toxicity and studies of hIAPP amyloid inhibitors are discussed.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107565"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145880389","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":"Recent developments and applications of photothermal AFM-IR in characterization of amyloids and amyloids aggregation processes: Mini-review","authors":"Quentin Machiels ,&nbsp;Céline Duchateau ,&nbsp;Jehan Waeytens","doi":"10.1016/j.bpc.2025.107551","DOIUrl":"10.1016/j.bpc.2025.107551","url":null,"abstract":"<div><div>AFM-IR combinates atomic force microscopy and infrared spectroscopy to compensate the limitations of both techniques taken separately. It has been reviewed for a large application field like polymers, geology and life sciences. In biology, it is an important tool to study amyloids and protein aggregation processes. Indeed, misfolding can appear under various circumstances in the process of globular proteins folding. In the case of amyloidosis, fibrillar aggregates are deposited in intracellular inclusions or in tissues as extracellular plaques. These aggregates (oligomers or fibrils) are characterized by high β-sheet content which can be analyzed in AFM-IR thanks to specific absorption band. The main progresses and developments of this technique are summarized since its creation in 2005. The evolution of laser sources and new measurement modes has led to the development of new instruments. They are always more efficient, allowing faster analysis, a wider sample range or more sensitive in order to give more (chemical) information about the sample. An overview of the progress made in photothermal AFM-IR in characterization of amyloids and amyloid aggregation processes is also described. The tapping and resonance-enhanced contact AFM-IR are the most commonly used modes. Generally, the label-free analysis of the conformation of the oligomers and/or fibrils at micromolar concentration is described, either in an aggregation kinetic study or in analysis of fibrils in <em>ex vivo</em> study. The coaggregation of two amyloids is also realized using ¹³C-labeled peptide to distinguish both two spectral signatures.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107551"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145676423","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":"Protonation and protein folding: Insights from single-molecule fluorescence","authors":"Vivek Pandey ,&nbsp;Nikky Sharma ,&nbsp;Tejasvi Pandey ,&nbsp;Rajinder Singh Kaundal","doi":"10.1016/j.bpc.2025.107564","DOIUrl":"10.1016/j.bpc.2025.107564","url":null,"abstract":"<div><div>Protein folding and protonation are deeply interconnected. Changes in the charge states of ionizable residues alter the local electrostatics and effective pKa values, influencing how proteins navigate their conformational landscapes. These protonation events can stabilize intermediates, guide folding pathways, and introduce kinetic diversity that support functional adaptability. Thus, understanding folding–protonation coupling has become a major focus of protein science. To probe these complex dynamics, increasingly sophisticated methodologies are required. Among them, single-molecule fluorescence (SMF) techniques have emerged as particularly powerful tools, providing unprecedented resolution of folding processes coupled to protonation. Approaches such as smFRET, fluorescence lifetime analysis, and rapid pH-jump experiments make it possible to observe events in exquisite detail. They reveal intermediates that escape detection in ensemble studies, capture heterogeneous subpopulations, and uncover rare, transient events that are critical to biological function. Building on these methodological advances, several case studies illustrate how protonation shapes biological outcomes for instance, histidine-rich domains function as molecular pH sensors, viral fusion proteins exploit protonation-triggered folding to mediate host entry, and engineered bio-switches harness pKa-dependent transitions to create adaptive biomaterials. When integrated with theoretical modeling, single-molecule data provide a coherent framework that links protonation dynamics to folding mechanisms across timescales. Here, in this review, we have not only consolidated current knowledge but also identified key gaps, particularly in connecting molecular-level protonation events with cellular and pathological contexts. By bridging these dimensions, this perspective aims to inspire new strategies in biomolecular engineering, therapeutic design, and the development of responsive functional materials.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107564"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145787369","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":"Novel heterocyclic hybrids of Thiophene clubbed 1,3,4-oxadiazoles targeting dihydrofolate reductase (DHFR): An in silico approach, molecular docking, ADMET studies, MM-GBSA assay and MD simulations","authors":"S. Prasanth ,&nbsp;B.C. Revanasiddappa ,&nbsp;Venkatesh Ranjan ,&nbsp;Durgesh Paresh Bidye ,&nbsp;Sheshagiri R. Dixit","doi":"10.1016/j.bpc.2025.107553","DOIUrl":"10.1016/j.bpc.2025.107553","url":null,"abstract":"<div><div>Nowadays Antimicrobial resistance (AMR) is considered as one of the major global concern and has become the leading confront since bacteria is continuously involved in the development of resistance against the diversified class of antimicrobial agents. Therefore, there is an urgent demand to find the new inhibitors and targets to overcome this problem. Dihydrofolate reductase (DHFR) is considered as one of the key enzyme, which plays a major role in supporting bacterial growth and hence these inhibitors were found to be highly effective therapeutic agents in combating bacterial infections. In this present study, Thiophene-clubbed 1,3,4-oxadiazoles derivatives (T1–15) were designed as potential DHFR inhibitors by in silico approach. We investigated 99 compounds as potential inhibitors of DHFR and the top 15 compounds were further selected for molecular docking studies. By using Schrodinger Maestro all the compounds were subjected to molecular docking study against the DHFR target (PDB:<span><span>1DG5</span><svg><path></path></svg></span>). The compounds T1 (‐8.206 kcal/mol) and T2 (−7.701 kcal/mol) exhibited highest docking scores when compared to the standard Trimethoprim (−6.482) and adhered to Lipinski rule for drug likeness, ADMET and toxicity profile. The MM-GBSA analysis indicated stable binding free energies. MD simulations have been performed for compound T1 and Trimethoprim to determine the stability of the complex for 200 ns. Overall, this research lays the groundwork in the development of novel class of DHFR inhibitors.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107553"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145683343","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":"Microwave-assisted green synthesis of (Co, Gd) dual doped ZnO nanoparticles using Phyllanthus emblica extract and their applications","authors":"Nirdosh Verma ,&nbsp;Dinesh Pathak ,&nbsp;Kamal Jeet ,&nbsp;Lacy Loveleen ,&nbsp;Surendra Nimesh ,&nbsp;Sunil Kumar ,&nbsp;Naveen Thakur","doi":"10.1016/j.bpc.2025.107554","DOIUrl":"10.1016/j.bpc.2025.107554","url":null,"abstract":"<div><div>This study reports a microwave-assisted green synthesis of cobalt and gadolinium dual doped ZnO nanoparticles using <em>Phyllanthus emblica</em> extract as a natural bio-stabilizer. The plant-derived phytochemicals enabled an eco-friendly process and improved nanoparticle stability. Structural, morphological, and optical analyses (TEM, XRD, SEM, EDX, UV–Vis) confirmed the successful formation of uniformly dispersed nanoparticles. The crystallite size obtained from XRD decreased from 26.59 to 20.59 nm with increasing Gd content, while TEM analysis showed slightly larger particle sizes ranging from 28.39 to 23 nm, validating the nanoscale dimensions and doping-induced size reduction. The (Co, Gd) dual doped ZnO nanoparticles exhibited strong antibacterial and antioxidant activity, demonstrating their potential to mitigate oxidative stress. Their photocatalytic efficiency was further confirmed through up to 97% degradation of Methyl Orange and Methylene Blue dyes. These combined results demonstrate that green synthesis and dual doping synergistically enhance the functional properties of ZnO nanoparticles, positioning them as promising candidates for environmental remediation, healthcare applications, sunscreen formulations, and active food packaging systems.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107554"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145645777","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":"Hydration parameters (h values) of hydrophobic l-amino acids estimated using the viscosity B-coefficients and partial molar volumes, and the low sensitivity of macromolecular interactions of xanthan gum on the effect of these amino acids in water","authors":"Yukinori Sato","doi":"10.1016/j.bpc.2025.107549","DOIUrl":"10.1016/j.bpc.2025.107549","url":null,"abstract":"<div><div>Hydration parameter <em>h</em> values of the hydrophobic <span>l</span>-amino acids (<span>l</span>-alanine, <span>l</span>-valine, <span>l</span>-leucine, <span>l</span>-isoleucine, and glycine as a reference) were estimated in water using the viscosity <em>B</em>-coefficients and partial molar volumes, and the food macromolecular interactions were explored in aqueous solutions at 25 °C using the apparent viscosities of macromolecular solutions (polyethylene glycol 3500, dextran T40, guar gum, locust bean gum, apple pectin, citrus pectin, sodium alginate, and xanthan gum) with <span>l</span>-amino acids (<span>l</span>-alanine, <span>l</span>-valine, and glycine as a reference). An increased number of hydrophobic groups were associated with viscosity <em>B</em>-coefficient values, the partial molar volume values, and hydration of approximately 1.4 mol of water per carbon-equivalent. When hydrophobic <span>l</span>-amino acids were added to food macromolecular solutions, the relationship between the apparent viscosity and amino acid molality could be expressed using linear regression lines; the slopes of these lines may reflect macromolecular interactions. Using this novel parameter, the contributions of the hydrophobicity of amino acids to macromolecular interactions can be compared. Glycine decreased and <span>l</span>-valine increased the apparent viscosities of almost all polyelectrolytes (i.e., pectins and alginate) in water, but the effects on nonelectrolytes were less marked (guar gum with glycine is an exception). The effects of <span>l</span>-alanine varied. However, these amino acids did not change the viscosity of xanthan in water, although xanthan is a polyelectrolyte. Thus, the low sensitivity of macromolecular interactions of xanthan gum on the effect of these hydrophobic <span>l</span>-amino acids has been demonstrated to be favorable for use as a stable food thickener.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"330 ","pages":"Article 107549"},"PeriodicalIF":2.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145712983","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 assessment of protein stability in ethanol-stressed environments via UV absorption and fluorescence spectroscopies","authors":"Erşed Akyüz ,&nbsp;Mikhail M. Vorob'ev ,&nbsp;Günnur Güler","doi":"10.1016/j.bpc.2025.107538","DOIUrl":"10.1016/j.bpc.2025.107538","url":null,"abstract":"<div><div>Maintaining the structure and functionality of proteins is crucial in applications ranging from food preservation to pharmaceutical formulation. Ethanol, while commonly used as a solvent and preservative, can induce structural changes in proteins depending on its concentration and the specific structure of the protein itself. This study investigates the structural effects of ethanol on three types of model proteins, namely bovine serum albumin (BSA), β-Lactoglobulin (β-Lg), and β-Casein (β-Cn), by using UV–Vis spectroscopy and fluorescence spectroscopy. The conformational responses of proteins in water-EtOH solutions of various ethanol concentrations (0–10 %, <em>v</em>/v) were analyzed through absorbance and emission spectral changes. At increasing ethanol concentration, UV absorption data showed distinct protein-dependent spectral changes. β-Lg and β-Cn exhibited strong hypochromism (an absorbance decrease of ∼25 %) and red-shifting at 222 nm and 220 nm, respectively, indicating partial unfolding and solvent exposure of aromatic residues. BSA demonstrated subtle changes, and consistent quenching in fluorescence with a continuous blue-shifting to 330 nm, suggesting a moderate overall stability and local rearrangements in its structure. β-Cn exhibited red-shifted fluorescence and quenching, reflecting its flexible, disordered structure and heterogeneous response to solvent conditions. Statistical analysis revealed that while fluorescence spectroscopy was highly sensitive to the intrinsic differences between proteins (<em>p</em> &lt; 0.001), the ethanol-induced conformational changes were too subtle to be detected as a statistically significant treatment effect. The consistency of these trends indicates a rational underlying mechanism of interaction. This reflects the subtle nature of the effect at the tested concentrations rather than the absence of an effect. Moreover, these results unveil the protein-specific effects of ethanol and strongly emphasize the importance of solvent composition in maintaining protein integrity. Ethanol concentrations up to 5 % may offer protein stability whereas high ethanol levels (≥ 5–10 %) promote structural perturbations. These results will be useful for both basic scientific research, such as biophysical studies and the advancement of optical techniques, and various industrial uses.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"329 ","pages":"Article 107538"},"PeriodicalIF":2.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145335032","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":"Backbone equilibrium in mismatched DNA influenced by solution conditions","authors":"A. Pilarski ,&nbsp;Gary A. Meints","doi":"10.1016/j.bpc.2025.107548","DOIUrl":"10.1016/j.bpc.2025.107548","url":null,"abstract":"<div><div>The impact of solution conditions on the ³¹P isotropic chemical shifts of DNA phosphates and therefore the sequence-dependent backbone conformational equilibrium has not been well-documented. There are no previous studies of DNA backbone equilibrium in the presence of crowding agents, nor any on mismatched DNA. A systematic study of several experimental conditions (Na⁺ concentration, K⁺ concentration, Mg²⁺ concentration, pH, the presence of PEG molecular crowders) was performed and the effect quantified in mismatched DNA compared to a canonical control sequence. Na⁺ concentration, pH and crowding agents have only a minimal effect on the backbone equilibrium (&lt;5 % perturbation on backbone populations). But in the mismatched DNA, both K⁺ and Mg²⁺ shift the backbone equilibrium on both DNA strands but most significantly perturb the phosphates in proximity to the mismatch. This indicates a possible role of counterions in mismatch recognition or nucleotide flipping, and suggests knowledge of solutions conditions continue to be relevant for conformational processes.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"329 ","pages":"Article 107548"},"PeriodicalIF":2.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145463778","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}