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A song of heads and tails: myosin II conformational regulation and filament dynamics shape force generation in non-muscle cells. 首尾之歌:非肌肉细胞中肌球蛋白II构象调节和丝动力学形状力的产生。
IF 5
Biophysical reviews Pub Date : 2026-03-10 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01414-1
Rafael Pérez-Díaz, Marina Garrido-Casado, Hugo Ramos-Solano, Clara Llorente-González, Vanessa C Talayero, Miguel Vicente-Manzanares
{"title":"A song of heads and tails: myosin II conformational regulation and filament dynamics shape force generation in non-muscle cells.","authors":"Rafael Pérez-Díaz, Marina Garrido-Casado, Hugo Ramos-Solano, Clara Llorente-González, Vanessa C Talayero, Miguel Vicente-Manzanares","doi":"10.1007/s12551-026-01414-1","DOIUrl":"10.1007/s12551-026-01414-1","url":null,"abstract":"<p><p>Non-muscle cells generate force without forming sarcomeres, building instead highly dynamic, contractile filaments that assemble, remodel, and disassemble in response to mechanical and biochemical signals. This review focuses on the conformational regulation and filament dynamics of myosin II paralogs as they define diverse types of cytoplasmic structures that produce mechanical forces. Whereas muscle myosin II stably resides in sarcomeres and conserve energy by adopting a super-relaxed state in which myosin II heads interact with each other and the core of the thick filament, smooth muscle and non-muscle myosin II shift between a soluble, folded, auto-inhibited 10S species and filaments, where they adopt an extended, assembly-competent 6S form. Phosphorylation of smooth muscle and non-muscle regulatory light chain triggers the conformational transition from 10S to 6S, leading to filament formation and contractile output. Other phosphorylations in the regulatory light and heavy chains also control filament assembly and dynamics through different molecular mechanisms. Biochemical and mechanical inputs fine-tune filament size, lifetime, and duty ratio, shaping contractile output across diverse cellular contexts. Upstream regulators, including biochemical and mechanical inputs, converge on several pathways, e.g., Ca<sup>2+</sup>/MLCK and RhoA/ROCK, organizing myosin II activity in space and time and enabling the emergence of stress fibers, junctional belts, cortical networks, and contractile rings that support adhesion, migration, cytokinesis, and tissue-level mechanics.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"201-220"},"PeriodicalIF":5.0,"publicationDate":"2026-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031461/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
High-frequency micro-viscoelasticity of biofluids by using optical trapping interferometry. 生物流体高频微粘弹性的光学捕获干涉测量。
IF 5
Biophysical reviews Pub Date : 2026-03-09 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01426-x
Pablo Domínguez-García
{"title":"High-frequency micro-viscoelasticity of biofluids by using optical trapping interferometry.","authors":"Pablo Domínguez-García","doi":"10.1007/s12551-026-01426-x","DOIUrl":"10.1007/s12551-026-01426-x","url":null,"abstract":"<p><p>Viscoelasticity is an essential characteristic of biomaterials like cells or tissues. The measurement of mechanical properties in biofluids requires experimental techniques using nanoscale local probe analysis and biological samples in small quantities. Optical trapping interferometry (OTI) tracks the Brownian motion of an optically trapped spherical microsphere, which explores the surrounding fluid driven by thermal energy. This technique provides a bandwidth in the microsecond range, which allows accessing the high-frequency regime in one-particle microrheology. In this paper, we review how the OTI equipment can be used to measure the micro-viscoelasticity of biofluids in the regime of high frequencies, in order to extract information about the dynamics of the individual biopolymers composing the material. We detail the implementation of this setup and its most recent applications in biophysics, alongside the development of the theory of Brownian motion and microrheology regarding the stochastic motion of the microprobe and the extraction of the mechanical properties of the fluid in which the particle is immersed.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"239-250"},"PeriodicalIF":5.0,"publicationDate":"2026-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031595/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572559","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Through the holes: the biotechnological potential of actinoporins (and other PFPs). 透过漏洞:放线素(和其他PFPs)的生物技术潜力。
IF 5
Biophysical reviews Pub Date : 2026-02-28 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01423-0
Javier Maraver-de-Paz, Diego Heras-Márquez, Juan Palacios-Ortega, Álvaro Martínez-Del-Pozo, Sara García-Linares
{"title":"Through the holes: the biotechnological potential of actinoporins (and other PFPs).","authors":"Javier Maraver-de-Paz, Diego Heras-Márquez, Juan Palacios-Ortega, Álvaro Martínez-Del-Pozo, Sara García-Linares","doi":"10.1007/s12551-026-01423-0","DOIUrl":"10.1007/s12551-026-01423-0","url":null,"abstract":"<p><p>Pore-forming proteins (PFPs) are singular polypeptides used by all kinds of organisms for attack or defence. They defy the stereotypical classification between water-soluble and membrane proteins. Within this large family of proteins, bacterial hemolysins and sea anemone actinoporins stand out as candidates for transforming these toxins into therapeutic or biotechnological devices. Over the past two decades, many examples have been published where these toxic proteins have been adapted to perform single-molecule tasks such as biosensing, sequencing of proteins and nucleic acids, discriminating protein chemical modifications, proteomics analyses, or even the use of DNA in computational approaches. Lately, PFPs have also been incorporated as templates for designing new artificial nanoreactors to catalyse different chemical reactions. A promising alternative within this idea is the recent publication of a proof of concept showing that actinoporins can be converted into biosustainable plastic-degrading nanoreactors. It is also discussed how optimisation and development of future PFP-based nanoreactors with improved activity and new specificities seem to be a venue worth to explore in order to degrade the contaminating waste material made of plastics from very different chemical compositions.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"221-238"},"PeriodicalIF":5.0,"publicationDate":"2026-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031482/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572487","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Why labelling the 'fast-reacting thiols' of myosin reduces force output: re-assessing a year at the University of California San Francisco (1987-8). 为什么标记肌球蛋白的“快速反应硫醇”会减少力量输出:重新评估加州大学旧金山分校的一年(1987-8)。
IF 5
Biophysical reviews Pub Date : 2026-02-27 eCollection Date: 2026-06-01 DOI: 10.1007/s12551-026-01425-y
Glenn Carrington, Michelle Peckham
{"title":"Why labelling the 'fast-reacting thiols' of myosin reduces force output: re-assessing a year at the University of California San Francisco (1987-8).","authors":"Glenn Carrington, Michelle Peckham","doi":"10.1007/s12551-026-01425-y","DOIUrl":"https://doi.org/10.1007/s12551-026-01425-y","url":null,"abstract":"<p><p>The fast-reacting thiol in the SH1 helix of myosin was often used to attach spin or fluorescent probes to the motor domain, to readout myosin orientation during the 1980s. However, at this time, we found that labelling this residue (Cys707) in myosin in skinned rabbit psoas fibres, using iodoacetacetamidotetramethyl rhodamine (IATR), reduced force output during active contraction. With access to recent pre- and post-powerstroke actomyosin structures, we can now explain these results. We modelled IATR onto the equivalent SH1 cysteine residue in the pre-power and post-power structures of myosin 5. This revealed that labelling of the fast-reacting thiol would interfere with the structural changes in the relay and SH1 helices required to generate the power stroke, explaining why force output reduces.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"627-631"},"PeriodicalIF":5.0,"publicationDate":"2026-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486406/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Call for papers for the special issue: celebrating the 90th anniversary of the Brazilian Biophysical Society (1936-2026). 特刊征文:庆祝巴西生物物理学会成立90周年(1936-2026)。
IF 3.7
Biophysical reviews Pub Date : 2026-02-26 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01421-2
Leandro R S Barbosa, Eneida De Paula, Antonio J Costa-Filho, Rosangela Itri
{"title":"Call for papers for the special issue: celebrating the 90<sup>th</sup> anniversary of the Brazilian Biophysical Society (1936-2026).","authors":"Leandro R S Barbosa, Eneida De Paula, Antonio J Costa-Filho, Rosangela Itri","doi":"10.1007/s12551-026-01421-2","DOIUrl":"https://doi.org/10.1007/s12551-026-01421-2","url":null,"abstract":"<p><p>The Brazilian Biophysical Society, SBBf, has played a pivotal role in advancing biophysics in Brazil and Latin America since its foundation in 1936. By promoting interaction among researchers and students through courses, meetings, conferences, and congresses, the Society has helped to consolidate biophysics as a respected discipline and fostered extensive collaborations. Therefore, to celebrate its 90<sup>th</sup> anniversary, a special issue of <i>Biophysical Reviews</i> will honor its legacy and highlight emerging trends and future directions in regional biophysical research.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"5-6"},"PeriodicalIF":3.7,"publicationDate":"2026-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031691/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572474","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Special issue "Biophysics in the Iberian Peninsula". 特刊“伊比利亚半岛的生物物理学”。
IF 3.7
Biophysical reviews Pub Date : 2026-02-24 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01422-1
Jorge Alegre-Cebollada, Germán Rivas
{"title":"Special issue \"Biophysics in the Iberian Peninsula\".","authors":"Jorge Alegre-Cebollada, Germán Rivas","doi":"10.1007/s12551-026-01422-1","DOIUrl":"10.1007/s12551-026-01422-1","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"1-4"},"PeriodicalIF":3.7,"publicationDate":"2026-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031700/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572547","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Nuclear magnetic resonance spectroscopy and membrane dynamics. 核磁共振波谱学和膜动力学。
IF 3.7
Biophysical reviews Pub Date : 2026-02-17 eCollection Date: 2025-12-01 DOI: 10.1007/s12551-026-01410-5
Michael F Brown
{"title":"Nuclear magnetic resonance spectroscopy and membrane dynamics.","authors":"Michael F Brown","doi":"10.1007/s12551-026-01410-5","DOIUrl":"https://doi.org/10.1007/s12551-026-01410-5","url":null,"abstract":"<p><p>Nuclear magnetic resonance (NMR) spectroscopy provides a unified framework for probing both the structure and dynamics of lipid membranes. In liquid-crystalline bilayers, orientational order parameters define the mean molecular organization, whereas nuclear spin-lattice relaxation rates report on fluctuations about this geometry. Combining solid-state <sup>2</sup>H NMR and <sup>13</sup>C NMR measurements allows a unified description of lipid bilayer structure and dynamics based on spectral lineshapes and on the dependence of relaxation rates on bilayer order parameters and resonance frequency. In the fluid phase, bilayers display short-range collective fluctuations similar to those of nematic liquid crystals, whereas longer-wavelength fluctuations are more characteristic of smectic-like behavior. Cholesterol-induced stiffening and surfactant-induced softening provide experimental signatures of quasi-elastic bilayer excitations. The enhanced relaxation observed in lipid membranes relative to hydrocarbon fluids is attributed to collective order-director fluctuations linked to membrane elastic deformation. By contrast, the local microviscosity remains comparable to that of liquid hydrocarbons of similar chain length. Solid-state NMR thus reveals the lipid bilayer as a membrane liquid crystal whose properties are shaped by lipid packing and elasticity, with important implications for peptide and protein interactions in cellular lipidomics.</p><p><strong>Graphical abstract: </strong></p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1697-1715"},"PeriodicalIF":3.7,"publicationDate":"2026-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957763/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147364042","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Biophysics of nanopore technologies: a roadmap for engineering protein channels as universal molecular sensors. 纳米孔技术的生物物理学:工程蛋白通道作为通用分子传感器的路线图。
IF 5
Biophysical reviews Pub Date : 2026-02-17 eCollection Date: 2026-04-01 DOI: 10.1007/s12551-026-01418-x
Aleksandr S Petrov, Vasiliy V Belov, Alexander V Sergeev, Maria I Zvereva
{"title":"Biophysics of nanopore technologies: a roadmap for engineering protein channels as universal molecular sensors.","authors":"Aleksandr S Petrov, Vasiliy V Belov, Alexander V Sergeev, Maria I Zvereva","doi":"10.1007/s12551-026-01418-x","DOIUrl":"https://doi.org/10.1007/s12551-026-01418-x","url":null,"abstract":"<p><p>Protein nanopores have evolved into a powerful biophysical tool, from direct DNA sequencing to versatile molecular sensors that detect RNA, proteins, aptamers, and low-molecular-weight analytes. This review summarizes the current state of nanopore technologies for biopolymer sequencing and metabolite detection and discusses prospects for developing universal sensors based on engineered protein channels. We trace the evolution of nanopore applications from reading genomic DNA to direct detection of diverse molecules, including RNA, proteins with post-translational modifications, and metabolites. We analyze key physicochemical parameters of the pore that determine selectivity and sensitivity and outline engineering strategies to optimize constriction geometry, charge patterning, signal-to-noise ratio, and stability. Mechanisms for controlled molecular translocation are considered, including enzyme-driven pulling, electroosmotic capture, and other motor-free approaches. Different membrane systems, from lipid bilayers to polymer and hybrid matrices, are compared in terms of protein compatibility, noise, and lifetime. We also describe advances in electronic readout, including parallel recording, integrated analog-to-digital conversion, adaptive sampling, and embedded real-time processing. Finally, we highlight emerging applications, from protein sequencing with modification mapping to multiplexed biomarker assays and hybrid nanopore devices, and discuss how modelling, de novo design, and directed evolution can accelerate the development of universal nanopore biosensors for biomedical diagnostics.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"307-325"},"PeriodicalIF":5.0,"publicationDate":"2026-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272708/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Mending the Achilles heels of titin in cardiac and musculoskeletal disease. 修复titin在心脏和肌肉骨骼疾病中的致命弱点。
IF 5
Biophysical reviews Pub Date : 2026-02-14 eCollection Date: 2026-02-01 DOI: 10.1007/s12551-026-01411-4
Ines Martinez-Martin, Roberto Silva-Rojas, Jorge Alegre-Cebollada
{"title":"Mending the Achilles heels of titin in cardiac and musculoskeletal disease.","authors":"Ines Martinez-Martin, Roberto Silva-Rojas, Jorge Alegre-Cebollada","doi":"10.1007/s12551-026-01411-4","DOIUrl":"10.1007/s12551-026-01411-4","url":null,"abstract":"<p><p>Titin, the largest known human protein, spans the sarcomere from Z-disk to M-line and is central to muscle elasticity, force transmission, and structural integrity. Maybe not surprisingly, accumulated evidence over the last years shows that titin, despite its titanic size, is not devoid of molecular <i>Achilles heels</i> that can lead to dysfunction and disease. In this review, we summarize the fundamental roles of titin in muscle mechanics, mechanosignaling, and physiology as well as in genetic and acquired disorders of cardiac and skeletal muscle. We discuss the current understanding of how mutations and posttranslational processing (dys)regulate titin, while highlighting gaps of knowledge regarding underlying molecular mechanisms. Finally, we analyze emerging experimental titin-cleavage models that are uncovering novel pathways of titin-based pathogenesis, positioning the protein not only as a central player in myocyte biomechanics but also as a determinant of pathological tissue remodeling. A main driving force in the field is to exploit the accumulated knowledge on titin to find new avenues for therapeutic intervention in cardiac and musculoskeletal disease.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"169-190"},"PeriodicalIF":5.0,"publicationDate":"2026-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031707/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572536","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Life and legacy in biophysics: 100th anniversary of Kechun Lin's birth. 生物物理学的生命与遗产:林克春诞辰100周年。
IF 5
Biophysical reviews Pub Date : 2026-02-13 eCollection Date: 2026-04-01 DOI: 10.1007/s12551-026-01419-w
Quanxiu Li, Cheng Zhen
{"title":"Life and legacy in biophysics: 100th anniversary of Kechun Lin's birth.","authors":"Quanxiu Li, Cheng Zhen","doi":"10.1007/s12551-026-01419-w","DOIUrl":"https://doi.org/10.1007/s12551-026-01419-w","url":null,"abstract":"<p><p>Kechun Lin (1926-2022) was an eminent biophysicist and educator, one of the earliest explorers of biophysics in China, and the year 2026 marks the centenary of his birth. He led to establish the Department of Biophysics at Beijing Medical College (now Peking University Health Science Center) in the 1950s as one of the earliest and most distinguished biophysical research centers in China. He co-founded the Biophysical Society of China, and advocated for its membership in the International Union for Pure and Applied Biophysics (IUPAB). He was the head of the delegation of the Biophysical Society of China to the International Biophysics Congress, and was elected and served for two consecutive terms as the IUPAB Councilor in the 1980s. His broad interests in biophysics covered lipid research, lipid-protein interactions, and medical issues related biomembranes.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"257-263"},"PeriodicalIF":5.0,"publicationDate":"2026-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272730/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275780","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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