Biophysical reviews最新文献

{"title":"The unconventional regulation of non-muscle myosins.","authors":"Andrew T Lombardo","doi":"10.1007/s12551-026-01437-8","DOIUrl":"10.1007/s12551-026-01437-8","url":null,"abstract":"<p><p>Myosins are actin-based molecular motors that power diverse forms of cellular motility across life. Initially characterized as the contractile machinery of muscle, the superfamily now includes numerous non-muscle classes with distinct cellular functions. Over the past decades, work across numerous actin-based systems has uncovered multiple modes of non-muscle myosin control. Recent advances now expand and, in some cases, challenge conventional regulatory paradigms, underscoring the complexity and adaptability of myosin function in cellular contexts. In this short review, I begin with a concise summary of the major canonical regulatory systems for non-muscle myosins. I follow this by highlighting the major novel regulatory findings from the last decade specifically relating to protein-binding partner activation, structural lipid-binding motifs, co-assembly of mixed classes of myosins, and the regulation of multi-motor complexes by the nanoscale organization of cellular actin. This review will appeal to the general scientific reader aiming to understand the mechanisms regulating myosins outside of the context of muscle and the current state of the non-muscle myosin field.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":" ","pages":""},"PeriodicalIF":5.0,"publicationDate":"2026-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13249394/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148216428","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}

{"title":"Spontaneous oscillatory contraction (SPOC) in striated muscle: focusing on mechanistic models.","authors":"Shin'ichi Ishiwata, Katsuhiko Sato, Naoaki Bekki","doi":"10.1007/s12551-026-01436-9","DOIUrl":"https://doi.org/10.1007/s12551-026-01436-9","url":null,"abstract":"<p><p>The contractile apparatus of striated muscle, including both skeletal and cardiac muscle, intrinsically exhibits self-sustained oscillatory behavior under intermediate activation states between contraction and relaxation. This phenomenon, termed SPOC (spontaneous oscillatory contraction), provides unique insights into the dynamic regulation of force generation. In this review, we first highlight experimental findings that characterize SPOC and then focus on theoretical frameworks developed to capture its essential features. A key feature of these models is the assumption that the lattice spacing, that is, the distance between the thick and thin filaments, varies dynamically during muscle contraction and that actomyosin activity depends on this spacing. This assumption naturally explains the emergence of SPOC. Particular attention is given to models constructed for single sarcomeres, isolated myofibrils, and small bundles of myofibrils, through which the underlying mechanisms of SPOC can be systematically understood. Finally, by extending the mathematical structure of these models, we propose that SPOC may exhibit chaotic properties, thereby providing a comprehensive understanding of its mechanisms and physiological significance.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"671-687"},"PeriodicalIF":5.0,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486431/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788089","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}

{"title":"<i>Biophysical Reviews</i>: a forum for publication of review articles from the international biophysics community.","authors":"Wilma K Olson","doi":"10.1007/s12551-026-01438-7","DOIUrl":"https://doi.org/10.1007/s12551-026-01438-7","url":null,"abstract":"<p><p>This Editorial introduces the contents of Volume 18, Issue 2 of <i>Biophysical Reviews</i>, the official journal of the International Union for Pure and Applied Biophysics (IUPAB). The broad scope of the articles in the Issue and the geographically widespread locations of the contributing authors mirror the goals of IUPAB, namely to organize worldwide advancements, co-operation, communication, and education in biophysics.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"251-254"},"PeriodicalIF":5.0,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272690/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276034","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}

{"title":"The thin line between biochemistry and structure where myosin super relaxed state lies.","authors":"Leonardo Nogara, Carlo Reggiani","doi":"10.1007/s12551-026-01433-y","DOIUrl":"https://doi.org/10.1007/s12551-026-01433-y","url":null,"abstract":"<p><p>This short review acknowledges the scientific contribution of Roger Cooke and colleagues, who first introduced the idea of two different biochemical states in resting skeletal muscle thick filament. In a seminal paper published in 2010, the state defined as myosin \"super relaxed state\" (SRX) has been proposed as the biochemical counterpart of the structural motif named interacting head motif (IHM). This connection has been challenged and revised multiple times, leading to misunderstandings and improper assumptions. In this review, we discuss the recent history of the structure-biochemistry relationship associated with resting myosin thick filament, its current interpretation, and how this is possibly related to future myosin resting state studies.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"633-640"},"PeriodicalIF":5.0,"publicationDate":"2026-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486409/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788046","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}

{"title":"Recollections of unraveling the molecular mechanism of force generation, and life, with Roger Cooke in the 1980s.","authors":"Brett Hambly, Piotr Fajer","doi":"10.1007/s12551-026-01434-x","DOIUrl":"https://doi.org/10.1007/s12551-026-01434-x","url":null,"abstract":"<p><p>The recent passing of Roger Cooke has led to many of his colleagues and friends reflecting on the substantial impact he made on both his chosen field of study, motility proteins, and the many colleagues he worked with. This brief memorial contribution remembers some of his early work, where, among many things, he was a world leader in developing and championing the use of electron paramagnetic resonance spectroscopy in the investigation of protein structure and dynamics, especially in complex protein arrays, such as muscle. We also include some more personal anecdotes that serve to illustrate the generosity and care that Roger extended to all those who worked with him, a true renaissance man of the twentieth century and beyond.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"597-599"},"PeriodicalIF":5.0,"publicationDate":"2026-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486423/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788101","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}

{"title":"Precision by design: Surface plasmon resonance and the integration of biophysics in fragment-based drug discovery.","authors":"Todd W Pascarella, Jeremiah S Joseph, Jason M Newman, Júlio C Borges, Paulo R Dores-Silva","doi":"10.1007/s12551-026-01429-8","DOIUrl":"https://doi.org/10.1007/s12551-026-01429-8","url":null,"abstract":"<p><p>Surface plasmon resonance (SPR) is a widely adopted and highly informative biophysical technique in fragment-based drug discovery, enabling the detection and characterization of weak and transient molecular interactions that initiate the progression from fragments to lead compounds. Owing to its sensitivity, low sample consumption, and compatibility with both direct-binding and functional assay formats, SPR plays a central role within integrated fragment discovery workflows, supporting affinity estimation, hit validation, and mechanistic interrogation when applied with appropriate experimental design. Recent advances in sensor-chip chemistries, buffer and solvent optimization, clean-screening strategies, and high-throughput instrumentation have further enhanced the robustness and reliability of SPR-based fragment assays. When combined with complementary biophysical and structural approaches, including thermal shift analysis, calorimetry, mass spectrometry, thermophoresis, NMR spectroscopy, X-ray crystallography, and cryo-electron microscopy, SPR contributes to a multidimensional validation framework that enables informed hit triage, structural interpretation, and structure-guided optimization. This review provides a practical guide to the use of SPR in fragment-based discovery, covering conceptual principles, experimental design, data analysis strategies, and best practices for minimizing artifacts and improving data quality. Beyond technical considerations, SPR illustrates a broader principle of molecular discovery: even weak interactions, when measured rigorously and interpreted in context, can yield insights that guide the transformation of fragment hits into biologically meaningful and therapeutically relevant molecules.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"363-387"},"PeriodicalIF":5.0,"publicationDate":"2026-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272721/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275941","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}

{"title":"Insight into the metabolism of gliomas by MRI and MRS.","authors":"Samishtha Pandey, Neha Yadav, Vivek Tiwari, Naranamangalam R Jagannathan","doi":"10.1007/s12551-026-01416-z","DOIUrl":"https://doi.org/10.1007/s12551-026-01416-z","url":null,"abstract":"<p><p>Gliomas are biologically and metabolically heterogeneous brain tumors whose clinical behavior is strongly influenced by lineage-defining genomic alterations such as isocitrate dehydrogenase (IDH1/2) mutation, 1p/19q-codeletion, ATRX loss, TERT promoter mutation, etc. Conventional magnetic resonance imaging (MRI) and tumor tissue biopsy are the clinical standards for diagnosis, tumor grading, and treatment planning. The conventional MRI/ magnetic resonance spectroscopy (MRS) identifies structural and vascular changes, and easy-to-measure high concentration metabolites. However, conventional MRS method suffers from spectral overlap and fails to provide a pure resonance, thus, it has limited application for estimation of difficult-to-identify and clinically relevant metabolic pool and flux changes in the tumors. Metabolic imaging using in vivo molecule tailored MRS provides a quantitative, highly precise non-invasive approach to measure tumor biochemistry in real time for ascertaining clinically relevant signatures for tumor diagnostication and prognostication. Recent developments in spectroscopic editing methods have provided quantitative MRS approaches to measure challenging metabolites such as glycine (Gly), glutamine (Gln), glutamate (Glu), 2-hydroxyglutarate (2HG), cystathionine and glutathione (GSH), in addition to routine MRS based measurements of metabolites, such as N-acetylaspartate (NAA), choline (Cho), creatine (Cr), lactate (Lac), etc. The pool of 2HG reflects epigenetic and redox remodeling in IDH-mutant tumors, whereas elevated glycine is associated with increased nucleotide demand and proliferative activity. Furthermore, molecule tailored MRS provide insights into cysteine-centered transsulfuration, antioxidant reprogramming and GSH-mediated radioresistance. Notably, these metabolic alterations often precede visible changes seen on anatomical MRI. Thus, metabolic profiling using molecule tailored MRS helps to find early tumor biomarkers for better diagnosis, along with the MRI. Future directions should include standardizing MRS protocols across imaging platforms, integrating metabolic markers with radio-genomics and machine-learning frameworks. Further, multi-center clinical trials and incorporating metabolic endpoints are necessary for adaptive therapy strategies. Together, MRI and MRS provide a comprehensive view of glioma biology that supports precision diagnosis, risk stratification, and individualized treatment planning, thereby advancing the goal of routine clinical adoption of metabolic imaging in neuro-oncology.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"511-526"},"PeriodicalIF":5.0,"publicationDate":"2026-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272710/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276079","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}

{"title":"Nano-based spectroscopic approaches for early diagnosis of Alzheimer's disease: critical insights into amyloid-β and tau biomarker biology and detection tools.","authors":"Andra-Sorina Tatar, Alia Colnita, Ioana-Andreea Brezestean, Sanda Boca","doi":"10.1007/s12551-026-01428-9","DOIUrl":"10.1007/s12551-026-01428-9","url":null,"abstract":"<p><p>Alzheimer's disease (AD) is the most prevalent neurodegenerative disorder, and its diagnosis relies primarily on symptoms that emerge long after irreversible neuronal damage. Early detection through reliable quantification of disease-associated protein biomarkers, particularly amyloid-β (Aβ) and tau species, remains a major unmet clinical need. Conventional immunoassays and imaging methods face significant limitations in sensitivity, cost, and suitability for large-scale decentralized screening, thus prompting interest toward nano-enabled spectroscopic biosensing approaches. This review critically examines nano-enabled spectroscopic approaches developed for the detection of Aβ and tau biomarkers, integrating biological context with technological innovation. We compare colloidal nanoparticle-based assays and solid-state nanostructured platforms, with emphasis on surface-enhanced Raman scattering (SERS) and related plasmonic techniques, as well as by the possibility of employing biorecognition strategies. Although many systems achieve ultra-low limits of detection under controlled conditions, we argue that analytical sensitivity alone is insufficient to ensure clinical relevance. Key translational challenges include fabrication reproducibility, batch-to-batch variability, standardization of enhancement metrics, validation in real biological matrices, and the absence of large clinical studies. The increasing incorporation of artificial intelligence for spectral analysis offers opportunities for improved classification, yet introduces concerns regarding dataset size and regulatory validation. By situating nano-spectroscopic biosensing within the biological complexity of early diagnosis of AD biomarkers and the practical constraints of clinical deployment, this review outlines the technological advances achieved to date and the critical steps required for translation: it will depend less on pushing detection limits further and more on achieving reproducibility, manufacturability, cost-effectiveness, and integration into standardized diagnostic workflows.</p><p><strong>Graphical abstract: </strong></p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"409-430"},"PeriodicalIF":5.0,"publicationDate":"2026-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272826/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275798","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}

{"title":"Insights from single-molecule force spectroscopy into chromatin topology.","authors":"Luuk J C Daris, Jorine M Eeftens","doi":"10.1007/s12551-026-01427-w","DOIUrl":"10.1007/s12551-026-01427-w","url":null,"abstract":"<p><p>The organization of DNA into chromatin within the eukaryotic nucleus represents one of the most intricate forms of biological packaging. This organization is inherently hierarchical, spanning multiple length scales: from DNA wrapping around histone octamers to form nucleosomes, to the folding of nucleosome arrays and the establishment of higher-order chromatin domains. Understanding how these scales interconnect is essential for explaining how cells regulate gene expression and replicate their genomes. Single-molecule force spectroscopy has provided powerful mechanistic insights into this architecture by enabling direct measurements of the forces that govern chromatin folding and unfolding. These approaches have clarified how chromatin fibers behave under tension and how nucleosome-level interactions contribute to fiber compaction and stability. In this review, we summarize key discoveries enabled by such techniques and discuss emerging opportunities for probing chromatin in increasingly complex and biologically relevant contexts.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"265-273"},"PeriodicalIF":5.0,"publicationDate":"2026-03-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272706/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276121","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}

{"title":"2026 Michèle Auger Award.","authors":"Wilma K Olson","doi":"10.1007/s12551-026-01424-z","DOIUrl":"https://doi.org/10.1007/s12551-026-01424-z","url":null,"abstract":"<p><p>This editorial introduces Nicholas M. I. Taylor, the winner of the 2026 Michèle Auger Award for Young Scientists' Independent Research.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 1","pages":"7-9"},"PeriodicalIF":3.7,"publicationDate":"2026-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13031674/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147572554","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}