European Biophysics Journal最新文献

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Specific TP53 mutations impair the recruitment of 53BP1 to DNA double-strand breaks underlying the mechanism of radioresistance. 特异性TP53突变损害53BP1对DNA双链断裂的招募,这是辐射耐药机制的基础。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-07-14 DOI: 10.1007/s00249-025-01774-8
Paolo Fagherazzi, Lenka Stixová, Eva Bartova
{"title":"Specific TP53 mutations impair the recruitment of 53BP1 to DNA double-strand breaks underlying the mechanism of radioresistance.","authors":"Paolo Fagherazzi, Lenka Stixová, Eva Bartova","doi":"10.1007/s00249-025-01774-8","DOIUrl":"https://doi.org/10.1007/s00249-025-01774-8","url":null,"abstract":"<p><p>The tumor suppressor p53, extensively studied for over 40 years, is a key regulator of various cellular pathways, often functioning independently of its transcriptional activity. Notably, p53 has been shown to play a crucial role in DNA repair, not only in sensing DNA damage but also in influencing repair pathway choice. This work assesses the influence of p53 on the recruitment and activity of the NHEJ mediator 53BP1, focusing specifically on common p53 hotspot mutations found in human cancers. The aim is to understand how these mutations impair DNA damage response mechanisms and contribute to genetic instability, which enhances tumor survival. Analysis of p53 missense mutations (R248W, R273C, G245S) revealed mutation-specific effects on 53BP1 and RIF1 recruitment, with G245S retaining wild-type-like 53BP1 recruitment but still exhibiting enhanced BRCA1 foci formation. Given the widespread activation of NHEJ throughout the cell cycle, especially in response to radiotherapy and chemotherapy, gaining insight into how p53 mutations affect this response is vital for developing future therapeutic strategies.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144635856","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Modifying recombinant purple acid phosphatase using computational design. 利用计算设计修饰重组紫色酸性磷酸酶。
IF 2.4 4区 生物学
European Biophysics Journal Pub Date : 2025-07-12 DOI: 10.1007/s00249-025-01779-3
Aishwarya Venkatramani, Montader Ali, Olga Predeina, Jennifer C Molloy, Pietro Sormanni, Elizabeth A H Hall
{"title":"Modifying recombinant purple acid phosphatase using computational design.","authors":"Aishwarya Venkatramani, Montader Ali, Olga Predeina, Jennifer C Molloy, Pietro Sormanni, Elizabeth A H Hall","doi":"10.1007/s00249-025-01779-3","DOIUrl":"10.1007/s00249-025-01779-3","url":null,"abstract":"<p><p>Enhancing protein stability while maintaining activity is a long-standing challenge in protein engineering, as modifications that benefit one property often compromise another. In this study, we leveraged a computational design strategy, CamSol Combination, to make a first step to improve the stability of purple acid phosphatase (PAP), a metalloprotein known for its distinctive pink color. PAP serves as a challenging model for engineering due to its complex redox-active site and the incorporation of iron ions critical to its function. Five mutations were introduced-H22R, A24P, F54P, H197P, and T208R-targeted to enhance thermal stability, as suggested by the computational design pipeline, while avoiding key functional regions. Experimental validation confirmed the choice of mutations with a 5 °C increase in thermal stability and retained enzymatic activity across a slightly expanded pH range. The mutations introduced subtle shifts in the enzyme's spectral and redox behavior, consistent with a lower energy of the oxidized state, and with dynamic light scattering data suggesting low aggregation. These results highlight the potential of computational approaches like the CamSol Combination to streamline protein engineering by enabling multi-trait optimization.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2025-07-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144615673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Optical trapping with nanostructured optical fibers and motility analysis of Pseudomonas aeruginosa 纳米结构光纤的光捕获及铜绿假单胞菌的动力学分析。
IF 2.4 4区 生物学
European Biophysics Journal Pub Date : 2025-07-08 DOI: 10.1007/s00249-025-01775-7
Eric Faudry, Jochen Fick
{"title":"Optical trapping with nanostructured optical fibers and motility analysis of Pseudomonas aeruginosa","authors":"Eric Faudry,&nbsp;Jochen Fick","doi":"10.1007/s00249-025-01775-7","DOIUrl":"10.1007/s00249-025-01775-7","url":null,"abstract":"<div><p>The study of bacteria swimming behavior or their interaction with other bacteria or cells requires an efficient and flexible tool for bacteria manipulation. Optical tweezers have been shown to be perfectly adapted for this task. Here we report optical trapping of pathogen <i>Pseudomonas aeruginosa</i> bacteria using optical fiber tweezers with dedicated nanostructured optical fibers. Well-aligned straight chains of up to ten bacteria were observed with optical fiber tips, whereas contactless trapping was realized at distances of 100 and 45 µm for Fresnel lens fibers and TIROFs, respectively. Very efficient trapping at laser powers as low as 3.7 mW was achieved. The bacteria vitality is an important parameter in trapping experiments. Mean square displacement and speed autocorrelation methods were applied to obtain a vitality measure and to classify the free bacteria trajectories into free floating, running, and run-wrap-run categories. The high frame rates of our observation videos allow us to reveal a relation between bacteria speed and bacteria orientation oscillations.</p></div>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":"54 5","pages":"277 - 287"},"PeriodicalIF":2.4,"publicationDate":"2025-07-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12310765/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144582774","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Unveiling the effect of curcumin on ion channels of SBMA motoneuron-derived cells and human IPSC-derived neurons: initial electrophysiological findings. 揭示姜黄素对SBMA运动神经元来源细胞和人ipsc来源神经元离子通道的影响:初步电生理发现。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-07-07 DOI: 10.1007/s00249-025-01780-w
Vera Plakhova, Ingrid Battistella, Vladimir A Martínez-Rojas, Marta Marchioretto, Daniele Arosio, Linda Masello, Luciano Conti, Carlo Musio
{"title":"Unveiling the effect of curcumin on ion channels of SBMA motoneuron-derived cells and human IPSC-derived neurons: initial electrophysiological findings.","authors":"Vera Plakhova, Ingrid Battistella, Vladimir A Martínez-Rojas, Marta Marchioretto, Daniele Arosio, Linda Masello, Luciano Conti, Carlo Musio","doi":"10.1007/s00249-025-01780-w","DOIUrl":"https://doi.org/10.1007/s00249-025-01780-w","url":null,"abstract":"<p><p>Curcumin (CUR), a bioactive compound extracted from the turmeric (Curcuma longa), has gathered considerable attention in recent years due to its claimed health benefits, including anti-inflammatory, antioxidant, and neuroprotective properties. The dysregulation of ion channel activity and the altered neuronal excitability in neurons has been identified as a key factor in the pathophysiology of neurological disease and a putative pharmacological target for therapeutic options. Therefore, we investigated by whole-cell patch-clamp the CUR's impact on the ionic currents in motoneuron-derived (MN-1) cells modeling SBMA and in human neuro-progenitor-cell (hNPCs)-derived neurons. CUR decreased viability in non-pathological MN-1 cells but showed increased resistance in pathological MN-1 cells, while mature neurons derived from hiPSCs remained unaffected under the same conditions. Electrophysiological studies revealed that CUR inhibits outward and inward currents in both MN-1 cell types, with a more pronounced effect in pathological cells. In hNPC-derived neurons, CUR also inhibited both currents and induced a negative shift in the voltage dependence of activation, suggesting reduced excitability. Our results indicate that further investigations are needed to confirm the role of CUR in the context of neurotherapeutics based on ion channel-targeting pharmacology.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144582775","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Modulation of conformational features and oligomerization of MMACHC by cobalamin variants: impact of the R161Q mutation in cblC disease. 钴胺素变异对MMACHC构象特征和寡聚化的调节:R161Q突变对cblC疾病的影响
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-06-27 DOI: 10.1007/s00249-025-01777-5
Lisa Longo, Maria Assunta Costa, Rita Carrotta, Maria Rosalia Mangione, Vincenzo Martorana, Marco Tutone, Maria Grazia Ortore, Paula M Garcia-Franco, Sonia Vega, Adrian Velazquez-Campoy, Rosa Passantino, Silvia Vilasi
{"title":"Modulation of conformational features and oligomerization of MMACHC by cobalamin variants: impact of the R161Q mutation in cblC disease.","authors":"Lisa Longo, Maria Assunta Costa, Rita Carrotta, Maria Rosalia Mangione, Vincenzo Martorana, Marco Tutone, Maria Grazia Ortore, Paula M Garcia-Franco, Sonia Vega, Adrian Velazquez-Campoy, Rosa Passantino, Silvia Vilasi","doi":"10.1007/s00249-025-01777-5","DOIUrl":"https://doi.org/10.1007/s00249-025-01777-5","url":null,"abstract":"<p><p>Vitamin B12 (cobalamin, Cbl) is a coordination compound of the cobalt, located at the center of a corrin ring composed of four pyrrolic-like groups. The cobalt ion can be bound to a variety of upper axial ligands, which vary among different cobalamin forms, including hydroxocobalamin (OHCbl), cyanocobalamin (CNCbl), methylcobalamin (MeCbl), and adenosylcobalamin (AdoCbl). MeCbl and AdoCbl are considered the biologically active forms, serving as cofactors in the metabolism of methylmalonic acid (MMA) and homocysteine (HCY). Impaired conversion of these metabolites leads to their pathological accumulation, resulting in severe cellular damage. This is precisely what occurs in cblC deficiency, a rare inborn disorder caused by mutations in the MMACHC protein, which plays a crucial role in binding and processing the various cobalamin forms. Mutations affecting MMACHC function impair its ability to correctly handle cobalamins, leading to the disease. In this study, we evaluated the impact of various cobalamin forms, specifically AdoCbl, MeCbl, and CNCbl, on the stability and oligomeric organization of the wild type MMACHC protein, using circular dichroism spectroscopy, native gel electrophoresis, and small-angle X-ray scattering. Moreover, isothermal titration calorimetry experiments provided insights into the thermodynamic parameters governing MMACHC binding to these cobalamins. In addition, we also assessed how the R161Q mutation in MMACHC alters the affinity of this protein for the different vitamin B12 forms, leading to decreased stability and impaired homodimerization, a process likely relevant to its functional role. Our findings provide molecular insights into cblC pathogenesis and advance our understanding of MMACHC structure-function relationships.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144504420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Inside the membrane: a closer look using elastic scattering techniques and friends. 薄膜内部:使用弹性散射技术和朋友更近距离观察。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-06-26 DOI: 10.1007/s00249-025-01761-z
Michael Kaltenegger, Enrico F Semeraro, Georg Pabst
{"title":"Inside the membrane: a closer look using elastic scattering techniques and friends.","authors":"Michael Kaltenegger, Enrico F Semeraro, Georg Pabst","doi":"10.1007/s00249-025-01761-z","DOIUrl":"https://doi.org/10.1007/s00249-025-01761-z","url":null,"abstract":"<p><p>Biological membranes are highly dynamic and adaptive interfaces that define cellular compartments, posing significant challenges for detailed characterization. Among the diverse range of experimental and computational techniques, small-angle scattering emerges as a label-free, non-invasive method capable of probing membrane structures across length scales from micrometers to subnanometers. By exploiting the complementary contrasts of X-ray and neutron scattering, combined with advanced optimization algorithms, this approach has provided unique insights into membranes with well-defined lipid and protein architectures. In this review, we highlight recent studies from the Pabst Lab, including investigations of lipid domains, asymmetric lipid membranes, and intrinsic lipid curvature. Furthermore, we explore the functional implications of these findings, such as the activity of an integral membrane enzyme and the effects of antimicrobial peptides in live cells. These examples underscore the versatility of small-angle scattering techniques in elucidating membrane functions, offering valuable perspectives for understanding cellular processes and advancing pharmaceutical applications.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144493357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Physical principles underpinning molecular-level protein evolution 支撑分子水平蛋白质进化的物理原理。
IF 2.4 4区 生物学
European Biophysics Journal Pub Date : 2025-06-26 DOI: 10.1007/s00249-025-01776-6
Jorge A. Vila
{"title":"Physical principles underpinning molecular-level protein evolution","authors":"Jorge A. Vila","doi":"10.1007/s00249-025-01776-6","DOIUrl":"10.1007/s00249-025-01776-6","url":null,"abstract":"<div><p>Since protein mutations are the main driving force of evolution at a molecular level, a proper analysis of the factors controlling them—such as the proteins’ robustness, the evolutionary pathways, the number of ancestors, the epistasis, the post-translational modifications, and the location and the order of mutations—will enable us to find a response to several crucial queries in evolutionary biology. Among them, we highlight the following: At the molecular level, what factors determine whether protein evolution is repeatable? Aiming at finding an answer to this and several other significant questions behind protein evolvability, we distinguish two evolutionary models in our analysis: convergent and divergent, based on whether or not a “target sequence” needs to be reached after <i>n</i> mutational steps beginning with a wild-type protein sequence (from an unknown ancestor). Preliminary results suggest—regardless of whether the evolution is convergent or divergent—a tight relationship between the thermodynamic hypothesis (or Anfinsen’s dogma) and the protein evolution at the molecular level. This conjecture will allow us to uncover how fundamental physical principles guide protein evolution and to gain a deeper grasp of mutationally driven evolutionary processes and the factors that influence them. Breaking down complex evolutionary problems into manageable pieces—without compromising the vision of the problem as a whole—could lead to effective solutions to critical evolutionary biology challenges, paving the way for further progress in this field.</p></div>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":"54 5","pages":"201 - 211"},"PeriodicalIF":2.4,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144504421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Quadruplexes with a grain of salt: influence of cation type and concentration on DNA G4 stability. 带盐颗粒的四联体:阳离子类型和浓度对DNA G4稳定性的影响。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-06-25 DOI: 10.1007/s00249-025-01772-w
Anne Cucchiarini, Filip Kledus, Yu Luo, Václav Brázda, Jean-Louis Mergny
{"title":"Quadruplexes with a grain of salt: influence of cation type and concentration on DNA G4 stability.","authors":"Anne Cucchiarini, Filip Kledus, Yu Luo, Václav Brázda, Jean-Louis Mergny","doi":"10.1007/s00249-025-01772-w","DOIUrl":"https://doi.org/10.1007/s00249-025-01772-w","url":null,"abstract":"<p><p>G-quadruplexes (G4) are stabilized by intra-quartet hydrogen bonds stacking between quartets, as well as specific and non-specific ionic interactions. Cation effects on G-quadruplexes differ significantly from those on duplexes, and specific cation coordination is indeed required to stabilize G4 structures. Most studies so far involve \"standard\" concentrations of potassium or sodium cations because of their prevalence in human cells, but several other monovalent and divalent cations may promote quadruplex formation. In addition, ionic strength may be different in other organisms such as Halophiles: the intracellular cation (potassium) concentration in salt-loving organisms such as Haloferax volcanii can be extremely high. In this study, we first performed a bioinformatics analysis of G4 propensity in halophiles and analyzed the impact of altering ionic strength or ionic balance on G4 or hairpin duplex stability. We then present a detailed and quantitative assessment of salt effect on a variety of duplex and quadruplex sequences. Over a dozen different quadruplex and duplex sequences were investigated by FRET melting and UV melting experiments. In addition, changes in sodium/potassium balance possibly occurring in human cells have a modest effect on G4-duplex competition. We also confirm that lithium is rather a \"G4-indifferent\" than a G4-destabilizing cation.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144482774","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Professor Emil Paleček: seven decades with electrodes and biomolecules at the Institute of Biophysics of the CAS. Emil paleek教授:在中国科学院生物物理研究所从事电极和生物分子研究70年。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-06-25 DOI: 10.1007/s00249-025-01771-x
Miroslav Fojta, Jan Paleček
{"title":"Professor Emil Paleček: seven decades with electrodes and biomolecules at the Institute of Biophysics of the CAS.","authors":"Miroslav Fojta, Jan Paleček","doi":"10.1007/s00249-025-01771-x","DOIUrl":"https://doi.org/10.1007/s00249-025-01771-x","url":null,"abstract":"<p><p>This year we celebrate seventy years since the establishment of the Institute of Biophysics of the Czechoslovak Academy of Sciences (IBP) (founded on January 1, 1955). If we look into the biography of Professor Emil Paleček (born on October 3, 1930), one of the most world-recognized personalities associated with the Institute and one of the most cited Czech scientists, known as the founder of nucleic acids electrochemistry, we are drawn to the same year, i.e. 1955, as the year in which Emil Paleček finished his studies in biochemistry and joined the IBP, where he worked with admirable vitality, enthusiasm and dedication until his death (October 30, 2018). In the context of celebration of founding of the Institute, we would like to commemorate in this article a personality who significantly influenced the history of the Institute alongside the important discoveries and research directions that defined his extremely successful career. We prefer this form, which is a sort of a mini-review of the most important results of the laboratory obtained under EP's leadership over 63 years, presented in mutual context and natural relations. For his life's work, Professor Paleček received many prestigious awards, with the Czech Head Award in 2014 and the Neuron Foundation Award in 2017 being the most distinguished.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144493358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Image analysis tools for improved characterization of nuclear chromatin patterns by confocal fluorescence microscopy. 通过共聚焦荧光显微镜改进核染色质模式表征的图像分析工具。
IF 2.2 4区 生物学
European Biophysics Journal Pub Date : 2025-06-23 DOI: 10.1007/s00249-025-01770-y
Mohammadmehdi Roushenas, Marco Salerno, Virginia Bazzurro, Elena Gatta, Alberto Diaspro
{"title":"Image analysis tools for improved characterization of nuclear chromatin patterns by confocal fluorescence microscopy.","authors":"Mohammadmehdi Roushenas, Marco Salerno, Virginia Bazzurro, Elena Gatta, Alberto Diaspro","doi":"10.1007/s00249-025-01770-y","DOIUrl":"https://doi.org/10.1007/s00249-025-01770-y","url":null,"abstract":"<p><p>We have collected fluorescence images of fixed cell nuclei of two different types-HeLa and HepG2-with DNA labeled by a standard fluorophore, and have devised three different quantitative parameters aimed to describe the distribution of the nuclear chromatin. The parameters are the fractal dimension, associated with the intricacy and hierarchical structure of chromatin; the total perimeter of local maxima, associated with the amount of chromatin domains; and the radial distance of angularly averaged intensity profile maximum, associated with the possible occurrence of a peak density at a characteristic distance from the nucleus center. Our results suggested that it was possible to differentiate the two types of cells in the 3D space of the defined parameters. Therefore, these parameters appear promising in identifying specific functional patterns in chromatin. At the same time, the negative control of different runs of measurements on the same cell type also showed at least partial differentiation. Thus, the tool proposed here for nuclear chromatin pattern characterization is probably sensitive to the cell life cycle moment almost as much as to the cell type and should be tested further on cells synchronized at the same phase during their cycle.</p>","PeriodicalId":548,"journal":{"name":"European Biophysics Journal","volume":" ","pages":""},"PeriodicalIF":2.2,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144473636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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