Hongzhen Su, Xuesong Lin, Li He, Chao Gao, Dezhao Zhang, Haotian Zhang, Daxue Du, Hong Liu, Wenzhong Shen
{"title":"Self-assembled conformal SnO2 electron transport layer via targeted chelating enables efficient, scalable, and stable perovskite solar cells","authors":"Hongzhen Su, Xuesong Lin, Li He, Chao Gao, Dezhao Zhang, Haotian Zhang, Daxue Du, Hong Liu, Wenzhong Shen","doi":"10.1016/j.xcrp.2025.102506","DOIUrl":"https://doi.org/10.1016/j.xcrp.2025.102506","url":null,"abstract":"","PeriodicalId":9703,"journal":{"name":"Cell Reports Physical Science","volume":"6 4","pages":"102506-102506"},"PeriodicalIF":0.0,"publicationDate":"2025-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147913559","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Fanchen Yu, Jinbo Fei, Yi Jia, Tonghui Wang, William F Martin, Junbai Li
{"title":"Chemiosmotic ATP synthesis by minimal protocells.","authors":"Fanchen Yu, Jinbo Fei, Yi Jia, Tonghui Wang, William F Martin, Junbai Li","doi":"10.1016/j.xcrp.2025.102461","DOIUrl":"10.1016/j.xcrp.2025.102461","url":null,"abstract":"<p><p>Energy conservation is crucial to life's origin and evolution. The common ancestor of all cells used ATP synthase to convert proton gradients into ATP. However, pumps generating proton gradients and lipids maintaining proton gradients are not universally conserved across all lineages. A solution to this paradox is that ancestral ATP synthase could harness naturally formed geochemical ion gradients with simpler environmentally provided precursors preceding both proton pumps and biogenic membranes. This runs counter to traditional views that phospholipid bilayers are required to maintain proton gradients. Here, we show that fatty acid membranes can maintain sufficient proton gradients to synthesize ATP by ATP synthase under the steep pH and temperature gradients observed in hydrothermal vent systems. These findings shed substantial light on early membrane bioenergetics, uncovering a functional intermediate in the evolution of chemiosmotic ATP synthesis during protocellular stages postdating the ATP synthase's origin but preceding the advent of enzymatically synthesized cell membranes.</p>","PeriodicalId":9703,"journal":{"name":"Cell Reports Physical Science","volume":"6 3","pages":"102461"},"PeriodicalIF":6.9,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11922820/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143691277","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Site-specific mutated albumin for covalently targeting NIR-II dye enables noninvasive imaging of blood-testis barrier integrity","authors":"Junrong Lin, Zetao Dang, Yijing Du, Yanli Gao, Jia Li, Yuewei Zhang, Shoujun Zhu","doi":"10.1016/j.xcrp.2025.102499","DOIUrl":"https://doi.org/10.1016/j.xcrp.2025.102499","url":null,"abstract":"<h2>Summary</h2> Assessing the integrity of the blood-testis barrier (BTB) is critical, as it serves to protect developing sperm cells by creating a protective environment against toxins and pathogens. Here, we optimize a near-infrared (NIR) dye for <i>in situ</i> binding of endogenous albumin or constructing NIR-II fluorescent proteins (FPs) based on exogenous albumin, affording non-invasive <i>in vivo</i> imaging of BTB disruption with tunable time windows. To further enhance the targeting capability of FPs, we employ a site-directed mutagenesis (SDM) strategy to develop the mutant albumin with increased binding efficiency to CO-1080 at room temperature, which serves as a specialized exogenous albumin for accelerating the imaging window of BTB disruption. Given the common drawbacks of traditional modalities for assessing BTB integrity, non-invasive and real-time NIR-II imaging is an effective method for investigating the testicular microenvironment as well as understanding testicular physiology and pathology.","PeriodicalId":9703,"journal":{"name":"Cell Reports Physical Science","volume":"6 3","pages":"102499-102499"},"PeriodicalIF":0.0,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147906060","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Wenyao Zhang, Christine E Harper, Junsung Lee, Bing Fu, Malissa Ramsukh, Christopher J Hernandez, Peng Chen
{"title":"Transporter excess and clustering facilitate adaptor protein shuttling for bacterial efflux.","authors":"Wenyao Zhang, Christine E Harper, Junsung Lee, Bing Fu, Malissa Ramsukh, Christopher J Hernandez, Peng Chen","doi":"10.1016/j.xcrp.2025.102441","DOIUrl":"10.1016/j.xcrp.2025.102441","url":null,"abstract":"<p><p>Multidrug efflux pumps confer not only antibiotic resistance to bacteria but also cell proliferation. In gram-negative bacteria, the ATP-binding cassette (ABC)-family transporter MacB, the adaptor protein MacA, and the outer membrane protein TolC form the MacA<sub>6</sub>:MacB<sub>2</sub>:TolC<sub>3</sub> assembly to extrude antibiotics and virulence factors. Here, using quantitative single-molecule single-cell imaging, we uncover that, in <i>E. coli</i> cells, there is a large excess of MacB (and TolC) driving the limiting adaptor protein MacA mostly into the MacAB-TolC assembly. Moreover, the excess MacB transporters can dynamically cluster around the assembly, and MacA can dynamically disassemble from the MacAB-TolC assembly, leading to an adaptor protein shuttling mechanism for efficient substrate sequestration from the periplasm toward efflux. We further show that both MacB clustering and MacAB-TolC assembly can be perturbed chemically or physically via microfluidics-based extrusion loading for compromised antibiotic tolerance. These insights may provide opportunities for countering the activities of multidrug efflux systems for antimicrobial treatments.</p>","PeriodicalId":9703,"journal":{"name":"Cell Reports Physical Science","volume":"6 2","pages":""},"PeriodicalIF":7.9,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11905320/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143623726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Membrane-assisted Aβ40 aggregation pathways.","authors":"Fidha Nazreen Kunnath Muhammedkutty, Huan-Xiang Zhou","doi":"10.1016/j.xcrp.2025.102436","DOIUrl":"10.1016/j.xcrp.2025.102436","url":null,"abstract":"<p><p>Alzheimer's disease (AD) is caused by the assembly of amyloid-beta (Aβ) peptides into oligomers and fibrils. Endogenous Aβ aggregation may be assisted by cell membranes, which can accelerate the nucleation step enormously, but knowledge of membrane-assisted aggregation is still very limited. Here, we used extensive molecular dynamics (MD) simulations to structurally and energetically characterize key intermediates along the membrane-assisted aggregation pathways of Aβ40. Reinforcing experimental observations, the simulations reveal unique roles of GM1 ganglioside and cholesterol in stabilizing membrane-embedded β sheets and of Y10 and K28 in the ordered release of a small oligomeric seed into solution. The same seed leads to either an open-shaped or R-shaped fibril, with significant stabilization provided by inter- or intra-subunit interfaces between a straight β sheet (residues Q15-D23) and a bent β sheet (residues A30-V36). This work presents a comprehensive picture of membrane-assisted aggregation of Aβ40, with broad implications for developing AD therapies and rationalizing disease-specific polymorphisms of amyloidogenic proteins.</p>","PeriodicalId":9703,"journal":{"name":"Cell Reports Physical Science","volume":"6 2","pages":""},"PeriodicalIF":7.3,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11905421/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143623724","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}