Biophysical reviewsPub Date : 2025-12-10eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01395-7
David N Langelaan
{"title":"Ian C. P. Smith-cofounder and driving force behind the Biophysical Society of Canada.","authors":"David N Langelaan","doi":"10.1007/s12551-025-01395-7","DOIUrl":"https://doi.org/10.1007/s12551-025-01395-7","url":null,"abstract":"<p><p>Ian C. P. Smith was a pioneer of biophysics in Canada and both a cofounder and driving force behind the Biophysical Society of Canada (BSC). His efforts and influence ultimately helped make the BSC the dynamic organization that it is today.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1681"},"PeriodicalIF":3.7,"publicationDate":"2025-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957662/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147364083","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":"Navigating the labyrinth of drugging the disordered.","authors":"Simran Tolani, Debarghya Mitra, Sarath Chandra Dantu, Ashutosh Kumar","doi":"10.1007/s12551-025-01391-x","DOIUrl":"https://doi.org/10.1007/s12551-025-01391-x","url":null,"abstract":"<p><p>Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are central players in many cellular processes, which make their involvement across cellular dysregulation and diseases evident. Unlike structured proteins, they carry out their functions mainly through interactions with a variety of partners. Recent progress, from large-scale proteome studies to detailed atomic-level investigations, has shed light on how their dynamic nature shapes complex structure-function relationships. Despite this flexibility, IDPs and IDRs are also being explored as promising drug targets. However, successful therapeutic efforts first require a careful understanding of their dynamic behavior and interactions. In this review, we outline how protein disorder influences both health and disease, and highlight relentless approaches aimed at turning this flexibility into opportunities for drug discovery.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"389-408"},"PeriodicalIF":5.0,"publicationDate":"2025-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272743/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275983","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}
Biophysical reviewsPub Date : 2025-12-08eCollection Date: 2026-04-01DOI: 10.1007/s12551-025-01381-z
Sreejith K P, Murukeshan Vadakke Matham, Santhosh Chidangil
{"title":"Recent developments in surface-enhanced Raman spectroscopy-based immuno (apta) assays for cardiac troponin detection: prospects for point-of-care applications.","authors":"Sreejith K P, Murukeshan Vadakke Matham, Santhosh Chidangil","doi":"10.1007/s12551-025-01381-z","DOIUrl":"10.1007/s12551-025-01381-z","url":null,"abstract":"<p><p>Cardiac troponin (cTn) is widely recognized as the gold standard for the diagnosis of acute myocardial infarction (AMI), a leading cause of mortality worldwide. Point-of-care testing (POCT) for cTn necessitates rapid turnaround, cost-effectiveness, user-friendly operation, and portability, along with the highest level of accuracy to support timely and effective clinical decision-making. Surface-enhanced Raman spectroscopy (SERS) based assays possess several features suitable for POCT, including the flexibility to integrate with innovative platforms such as microfluidic systems and paper-based devices. In this review, we discuss the recent developments in SERS-based immuno (apta) assays for cTn detection, with a focus on detection strategies, employed platforms, and their feasibility for POCT. This review also outlines the improvements required in existing assays to meet POCT requirements, aiding in the design of future diagnostic assays.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"431-457"},"PeriodicalIF":5.0,"publicationDate":"2025-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272741/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275938","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}
Biophysical reviewsPub Date : 2025-12-07eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01392-w
Scott B King
{"title":"Ian Cormack Palmer Smith-the supervisor.","authors":"Scott B King","doi":"10.1007/s12551-025-01392-w","DOIUrl":"https://doi.org/10.1007/s12551-025-01392-w","url":null,"abstract":"<p><p>Dr. Ian C.P. Smith was more than a mentor-he was my greatest supporter, and for that, I am deeply grateful.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1673"},"PeriodicalIF":3.7,"publicationDate":"2025-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957753/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147363995","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}
Biophysical reviewsPub Date : 2025-12-06eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01386-8
Moustafa Habes, Camille M Hénault, John E Baenziger
{"title":"Rapsyn-acetylcholine receptor interactions: structural models inform mechanisms of clustering at the neuromuscular junction.","authors":"Moustafa Habes, Camille M Hénault, John E Baenziger","doi":"10.1007/s12551-025-01386-8","DOIUrl":"https://doi.org/10.1007/s12551-025-01386-8","url":null,"abstract":"<p><p>Synaptic communication across the neuromuscular junction is mediated by high-density clusters of the nicotinic acetylcholine receptor (nAChR), with the initiation and maintenance of clustering facilitated by a peripheral membrane protein, rapsyn. Despite the importance of both the nAChR and rapsyn to neuromuscular junction formation and function, structural insight into the rapsyn-nAChR complex and thus how the formation of this complex facilitates clustering is still lacking. In this review, we update our current understanding of nAChR-rapsyn interactions in the context of new structures of the muscle-type nAChR, as well as computationally predicted models of both rapsyn and the nAChR-rapsyn complex. By integrating domain-function studies, biochemical data, and both new and predicted structural data, we present a plausible model of nAChR-rapsyn complex that provides a framework for understanding both clustering at the neuromuscular junction and how mutations in rapsyn lead to the neuromuscular disease, congenital myasthenic syndrome.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1749-1762"},"PeriodicalIF":3.7,"publicationDate":"2025-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957682/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147363987","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}
Biophysical reviewsPub Date : 2025-12-05eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01394-8
Manuel Prieto, Anthony Watts
{"title":"Ian C. P. Smith-a dynamic and enlightened president of the IUPAB.","authors":"Manuel Prieto, Anthony Watts","doi":"10.1007/s12551-025-01394-8","DOIUrl":"https://doi.org/10.1007/s12551-025-01394-8","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1679"},"PeriodicalIF":3.7,"publicationDate":"2025-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957702/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147364025","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}
Biophysical reviewsPub Date : 2025-12-02eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01390-y
Boguslaw Tomanek
{"title":"Ian Cormack Palmer Smith-the boss.","authors":"Boguslaw Tomanek","doi":"10.1007/s12551-025-01390-y","DOIUrl":"https://doi.org/10.1007/s12551-025-01390-y","url":null,"abstract":"<p><p>Ian C. P. Smith management's career began at the National Research Council of Canada in Ottawa as the Director General of the Institute for Biological Sciences. His research vision brought him to his beloved Winnipeg, where he established the Institute for Biodiagnostics dedicated to diagnostic applications of Magnetic Resonance, Infrared Spectroscopy, and Bioinformatics. He created a world-class research facility supporting the development of biotechnology and creating commercial opportunities in Canada. This commentary provides a perspective of from an employee of Ian as a supervisor, director, and manager.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1671-1672"},"PeriodicalIF":3.7,"publicationDate":"2025-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957672/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147364062","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}
Biophysical reviewsPub Date : 2025-12-01eCollection Date: 2025-10-01DOI: 10.1007/s12551-025-01388-6
Anastasia A Anashkina, Yuriy F Zuev, Konstantin S Usachev, Vladimir I Polshakov, Bogdan S Mel'nik, Yuriy L Orlov, Andrey B Rubin
{"title":"Biophysical Reviews special issue associated with the Russian Autumn School in Biophysics held in Kazan, Russia, 11-14 November 2024.","authors":"Anastasia A Anashkina, Yuriy F Zuev, Konstantin S Usachev, Vladimir I Polshakov, Bogdan S Mel'nik, Yuriy L Orlov, Andrey B Rubin","doi":"10.1007/s12551-025-01388-6","DOIUrl":"https://doi.org/10.1007/s12551-025-01388-6","url":null,"abstract":"<p><p>Overall, the school collected presentations on molecular biophysics and experimental techniques, addressed major unresolved challenges in the field, and shared an overall perspective on future directions that might help to clarify the important questions that emerged during the last decade of intensive research. To conclude, we note growing interest in AI applications for biophysical modeling, new physical experimental techniques such as cryo-microscopy, applications of modeling in pharmaceutical research, and drug design. We believe this special journal issue will be of interest to readers.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 5","pages":"1183-1186"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12847572/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146084256","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}
Biophysical reviewsPub Date : 2025-11-29eCollection Date: 2025-12-01DOI: 10.1007/s12551-025-01379-7
Daniel Garcia-Gonzalez
{"title":"Magneto-mechanics in mechanobiology: enabling remote force transmission to cells and extracellular matrix.","authors":"Daniel Garcia-Gonzalez","doi":"10.1007/s12551-025-01379-7","DOIUrl":"https://doi.org/10.1007/s12551-025-01379-7","url":null,"abstract":"<p><p>Mechanobiology explores how cells sense, transmit, and respond to mechanical forces, with the extracellular matrix (ECM) serving as a dynamic interface that governs cellular behavior through stiffness, viscoelasticity, poroelasticity, and topographical cues. Traditional techniques for force application, such as atomic force microscopy, micropipette aspiration, and optical tweezers, have provided foundational insights but are often limited in dimensionality, invasiveness, and capacity to mimic native, time-evolving microenvironments. Magneto-mechanical actuation offers a transformative alternative by enabling remote, reversible, and spatially programmable force delivery to cells and tissues via particle-based, substrate-based, or microrobotic platforms. This review examines ECM structure-function relationships, cellular mechanotransduction via the cytoskeleton and mechanosensitive ion channels, as well as the capabilities and constraints of existing mechanical probing tools. Magneto-mechanical modalities, design considerations, calibration strategies, and integration with real-time biological readouts are then detailed, highlighting their potential to reproduce complex, dynamic mechanical cues relevant to development, disease, and regeneration. Finally, current technical and biological challenges are discussed, proposing bioinspired actuation schemes for temporal mechanical conditioning, and envisioning multiphysics integration as a path toward next-generation mechanomedicine.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"17 6","pages":"1837-1862"},"PeriodicalIF":3.7,"publicationDate":"2025-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12957747/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147364056","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}
Biophysical reviewsPub Date : 2025-11-27eCollection Date: 2026-04-01DOI: 10.1007/s12551-025-01385-9
Joanna Lewandowska, Barbara Kalenik, Antoni Wrzosek, Bogusz Kulawiak, Piotr Bednarczyk, Barbara Zablocka, Adam Szewczyk
{"title":"Mitochondrial potassium channels: mitochondria-specific mechanism of regulation.","authors":"Joanna Lewandowska, Barbara Kalenik, Antoni Wrzosek, Bogusz Kulawiak, Piotr Bednarczyk, Barbara Zablocka, Adam Szewczyk","doi":"10.1007/s12551-025-01385-9","DOIUrl":"10.1007/s12551-025-01385-9","url":null,"abstract":"<p><p>Potassium channels identified in the plasma membrane play a crucial role, particularly in generating action potentials in excitable cells. Recently, potassium channels have also been discovered in intracellular organelles, including the inner mitochondrial membrane (IMM), which share many properties with their plasma membrane counterparts. Mitochondrial potassium channels exhibit similar biophysical, pharmacological, and regulatory characteristics, reflecting their common molecular origin. However, differences in potassium channel activity may result from differences in isoforms as well as from the specific ionic, protein, and lipid environments associated with their distinct subcellular locations. In particular, the IMM imposes unique conditions that shape the regulation of mitochondrial potassium channels. These include close proximity to the respiratory chain, high mitochondrial metabolic activity, a pronounced transmembrane potential, and pH gradients. This review examines how these mitochondrial-specific factors influence the function of mitochondrial potassium channels. A deeper understanding of how the IMM environment modulates mitochondrial channel activity will not only expand our knowledge of mitochondrial physiology but may also pave the way for new therapeutic strategies targeting mitochondrial dysfunction and the role of mitochondrial potassium channels in human diseases.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"327-337"},"PeriodicalIF":5.0,"publicationDate":"2025-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272845/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148275795","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}