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        <title>Frontiers in Biophysics | New and Recent Articles</title>
        <link>https://www.frontiersin.org/journals/biophysics</link>
        <description>RSS Feed for Frontiers in Biophysics | New and Recent Articles</description>
        <language>en-us</language>
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        <pubDate>2026-08-12T17:58:22.170+00:00</pubDate>
        <ttl>60</ttl>
        <item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1925801</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1925801</link>
        <title><![CDATA[Silent Kv subunits as major players in cell membrane excitability]]></title>
        <pubdate>2026-08-12T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Mohammed Alshemery</author><author>Mert Beyazyildirim</author><author>Joao L. Carvalho-de-Souza</author>
        <description><![CDATA[Silent Kv subunits are alpha subunits forming heteromeric Kv channels. These subunits do not form functional homomeric Kv channels, and their function in cell biology is realized when co-assembled with Kv2 subunits. There are currently 10 silent Kv subunits encoded in the genome of humans and other mammals, and they all produce biophysically unique voltage-gated potassium channels. KvS subunits are expressed in various tissues in the body, with tissue-specific distribution in many cases, where they fine tune cell excitability to keep homeostasis in health and disease. There are currently over 400 genome-wide association studies involving KvS subunits with traits and diseases. Although some statistics methods suggest parsimony when interpreting these populational data, it is undeniable that KvS-subunit-encoding genes, conserved part of the DNA, have important roles in biology. KvS subunits are unexplored as molecular targets. This perspective paper proposes to serve as a valuable resource for upcoming, detailed studies of these heteromeric channels, particularly focusing on the gating-related molecular mechanisms of the KvS subunits.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1870174</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1870174</link>
        <title><![CDATA[Probing peptide-mediated membrane pore formation by fluorescence, infrared spectroscopy, and atomic force microscopy]]></title>
        <pubdate>2026-08-06T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Suren A. Tatulian</author><author>Munira Haque</author>
        <description><![CDATA[Membrane pores and channels play key roles in cell physiology. Hence, the elucidation of their structure is important for understanding their molecular mechanisms and for designing drugs to recover their impaired function during various pathologies. Atomic resolution structural techniques such as X-ray crystallography or nuclear magnetic resonance have made strides in studying membrane proteins but still encounter difficulties due to resistance to crystallization and the large size of protein-membrane complexes. Other biophysical methods are being employed to tackle these proteins. The focus of this article is on three such approaches, i.e., fluorescence, Fourier transform infrared spectroscopy, and atomic force microscopy. The application of these techniques to characterize ion conducting pore formation by various peptides in lipid bilayers is described. Combined, these approaches provide comprehensive information on pore structure and function such as the kinetics of pore assembly, pore size, stoichiometry, peptide-peptide affinities, the secondary structure, depth of membrane insertion, the orientation of the pore-forming peptide molecules with respect to the membrane, and the supramolecular morphology of the membrane-embedded functional pore.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1781425</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1781425</link>
        <title><![CDATA[Targeting cancer matrix mechanics: fibronectin fiber relaxation correlates with ADAM8 expression in PDAC and is amenable to in vitro modulation]]></title>
        <pubdate>2026-08-06T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Konstantin M. P. Wolf</author><author>Lea S. Ottenwald</author><author>Martin Wartenberg</author><author>Mamta Chabria</author><author>Viola Vogel</author>
        <description><![CDATA[Pancreatic ductal adenocarcinoma (PDAC) is among the deadliest cancers, characterized by a dense desmoplastic stroma rich in extracellular matrix (ECM) that impairs therapy and promotes tumor progression. Fibronectin (FN), a major ECM component, provides binding sites for growth factors and integrins, and changes in its mechanical signature have been associated with the progression of several pathologies, including the invasiveness of breast cancer. Using the mechano-sensitive peptide probe FnBPA5, which binds relaxed FN fibers, we mapped FN fiber tension in cryosections from PDAC patient biopsies by comparing tumor regions to matched non-cancerous tissue. Even though counterintuitive, tumor stroma was strongly enriched in untensed FN fibers, whereas non-cancerous tissue showed minimal FnBPA5 binding. Untensed FN fibers localized near alpha smooth muscle actin (αSMA)-positive myofibroblastic cancer-associated fibroblasts (myCAFs) and collagen triple helix repeat containing 1 (CTHRC1)-positive stromal cells and correlated strongly with a disintegrin and metalloproteinase domain-containing protein 8 (ADAM8), a FN-cleaving protease. In 2D culture, healthy pancreatic stellate cells (PSCs) adopted a myCAF-like phenotype when exposed to PANC-1 cancer cells, as shown by αSMA and CTHRC1 upregulation, and assembled an ECM enriched in relaxed FN fibers. Supplementation with standard PDAC chemotherapeutics (paclitaxel or gemcitabine) and addition of ADAM8 inhibitors to PSCs partially reversed loss of FN fiber tension in vitro. Together, our findings establish untensed FN fibers as a hallmark of PDAC stroma and present a minimal in vitro model to probe and modulate ECM fiber mechanics for disease-specific drug screening.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1926644</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1926644</link>
        <title><![CDATA[Editorial: Structural and functional roles of membrane transport proteins in cellular physiology]]></title>
        <pubdate>2026-07-24T00:00:00Z</pubdate>
        <category>Editorial</category>
        <author>Olga Vinogradova</author>
        <description></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1769000</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1769000</link>
        <title><![CDATA[From scattering curves to structural descriptors: interpretable machine learning maps SAXS/WAXS signals to RNA structural details in defined RNA motifs]]></title>
        <pubdate>2026-07-14T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Weiwei He</author><author>Serdal Kirmizialtin</author>
        <description><![CDATA[Solution X-ray scattering offers an ensemble-averaged picture of biomolecular structure and dynamics under near-physiological conditions. Small-angle X-ray scattering (SAXS) reports on global architecture, while extending to the wide-angle regime (WAXS) captures sub-nanometer-level details. However, SAXS/WAXS (SWAXS) interpretation is complicated due to the overlap of multiple correlation lengths. Here, we present a machine-learning (ML) framework that infers structural properties for a given RNA fold. Using molecular simulations to generate ensembles, LightGBM (light gradient-boosting machine) successfully learns mappings from SWAXS features to key geometric properties. We apply this approach to double-stranded RNA (dsRNA) duplexes and a two-way junction construct. The models accurately predict structural changes from SWAXS data and highlight diagnostic q-windows that encode duplex and junction fingerprints. Our results demonstrate that interpretable ML trained on RNA structural ensembles provides a robust route to extract structural information from solution scattering measurements of RNAs.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1880887</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1880887</link>
        <title><![CDATA[Intrinsically disordered regions as drivers of protein aggregation: mechanisms, phase separation, and emerging predictive frameworks]]></title>
        <pubdate>2026-07-10T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Rahul Kaushik</author><author>Suyong Re</author>
        <description><![CDATA[Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack stable tertiary structures yet perform essential roles in cellular signaling, molecular recognition, transcriptional regulation, and biomolecular assembly. Their conformational flexibility enables functional adaptability but also increases susceptibility to aberrant intermolecular interactions and protein aggregation. Unlike folded proteins, aggregation in IDPs arises from transient conformational ensembles that expose cryptic aggregation-prone regions (APRs), facilitating oligomerization and fibril formation under specific cellular and environmental conditions. Several studies have further established a mechanistic relationship between intrinsic disorder, liquid–liquid phase separation (LLPS), and pathological aggregation, where dynamic condensates can undergo maturation into irreversible amyloid-like assemblies. These transitions are strongly influenced by sequence grammar, charge distribution, aromatic residue patterning, post-translational modifications, molecular crowding, and proteostasis regulation. This mini-review summarizes the molecular principles governing aggregation in disordered systems, with emphasis on conformational ensemble dynamics, disorder-to-order transitions, and the interplay between LLPS and fibrillization. The review further discusses computational approaches used to predict aggregation propensity in IDRs, including classical physicochemical predictors, ensemble-aware simulations, molecular dynamics frameworks, and emerging protein language model-based methods. Further, integration of artificial intelligence, structural biophysics, and multiscale modeling have substantially improved understanding of disorder-driven aggregation pathways. Collectively, these findings support a unified framework in which sequence composition, conformational heterogeneity, and cellular environment cooperatively regulate functional assembly and pathological aggregation in intrinsically disordered proteins.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1839006</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1839006</link>
        <title><![CDATA[Chromatic discrimination in protocells toward proto vision and intelligence]]></title>
        <pubdate>2026-07-08T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Panagiotis Mougkogiannis</author><author>Andrew Adamatzky</author>
        <description><![CDATA[Proteinoids—thermally synthesized amino acid copolymers—have long served as prebiotic chemistry models for protocell formation, yet their lack of dynamic responsiveness limits applications in smart biomaterials. We describe the synthesis and study of photoswitchable proteinoids. These include phenylalanine-4′-azobenzene hydrochloride chromophores. They were made through thermal polycondensation at 170–180 °C using glutamic acid and phenylalanine monomers. Scanning electron microscopy shows self-assembly into bowl-shaped structures, like stomatocytes. These structures range from 0.5 to 10 m in diameter. They form when the membrane collapses due to cooling and dehydration. UV-visible spectroscopy confirms azobenzene survival through thermal synthesis, with J-aggregate formation producing red-shifted absorption bands near 520 nm. Reversible photoswitching was confirmed by repeated UV–visible light cycling experiments, in which the 520 nm J-aggregate absorption band alternated between bleached (UV, trans→cis) and recovered (visible, cis→trans) states over at least five consecutive cycles, confirming that the observed electrophysiological responses are causally linked to photoisomerization rather than photodegradation or thermal artefacts. Electrophysiological tests at six wavelengths—blue, daylight, gray, green, red, and yellow—show that azobenzene-functionalized networks change voltage from −130 to +150 mV. In contrast, pure proteinoids stay mostly inactive. Multi-electrode mapping shows how photoresponsive areas are organized. Channels 13–14 and 15-16 have large polarity reversals, reaching up to 150 mV under yellow and green light. In contrast, channel 11–12 shows unique suppression. This creates different types of photodetection, similar to retinal photoreceptor mosaics. Electrochemical impedance spectroscopy shows a 49% drop in real impedance and a 35% drop in imaginary impedance in azobenzene-functionalized samples. This indicates better charge mobility. Cyclic voltammetry demonstrates 976% increased anodic current and 2181% enhanced charge storage capacity, confirming transformation into redox-active materials. Binary logic gate analysis shows AND-like behavior (75% agreement score). The output needs both azobenzene and light input. This demonstrates chemical Boolean operations through wavelength-selective photoisomerization. These photoswitchable proteinoids are self-assembled chemical systems. They can discriminate colors, process signals based on wavelength, and perform photonic logic. This suggests potential for light-controlled drug delivery, adaptive biosensors, and molecular computation platforms.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1677942</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1677942</link>
        <title><![CDATA[Threshold transitions of 15N fluxes reveal state-dependent root conductance and flux partitioning within steady-state nitrate isotherms]]></title>
        <pubdate>2026-06-08T00:00:00Z</pubdate>
        <category>Hypothesis and Theory</category>
        <author>Erwan Le Deunff</author><author>Philippe Malagoli</author>
        <description><![CDATA[This study reexamines Epstein’s ionic isotherms, arguing that the traditional enzyme-substrate interpretation, which assumes a coherent, continuous, and saturated response, has bypassed significant transition thresholds in root ion fluxes. We integrate new and published 15N tracer datasets obtained under homogeneous and heterogeneous nitrate supply conditions. The results show that transitions in root uptake (vin and vapp) and export to the shoot (vout) are strongly context-dependent. These findings suggest that a three-compartment soil-root-shoot model better explains biphasic nitrate isotherms than commonly-cited two-compartment approaches. Under all tested experimental conditions, the relationships between 15N fluxes and external concentrations exhibit clear, threshold-like regime switching. This is consistent with shifts in the dominance of radial versus longitudinal resistances within the root-shoot system. We propose that repeated radial units act as biological varistors - nonlinear, threshold-sensitive elements whose collective behavior depends on root architecture and nitrate distribution rather than fixed Km and Vm parameters. Varistor-like responses have been reported for X-QUAC channels and NRT1.1/NPF6.3-like transporters. Meanwhile, NRT2.1 and Ca2+-dependent CBL-CIPK signaling remain central to regime transitions. Using steady-state isotherms that focus on context-dependent regime changes, root structure, and threshold transitions provides a more realistic basis for interpreting nitrate uptake experiments, designing physiological studies, and developing breeding strategies that improve nitrogen use efficiency in variable environments.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1860065</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1860065</link>
        <title><![CDATA[Biomolecular condensation meets membrane biophysics: from interfacial physical principles to emerging therapeutic opportunities]]></title>
        <pubdate>2026-06-01T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Agustín Mangiarotti</author><author>Ernesto E. Ambroggio</author><author>M. Soledad Celej</author>
        <description><![CDATA[Biomolecular condensates are increasingly recognized as central organizers of cellular biochemistry, providing dynamic, self-assembled compartments that control reaction rates, molecular selectivity, and spatial organization. Beyond bulk cytoplasmic and nuclear phases, an emerging paradigm highlights condensates that form and operate at membrane interfaces, where protein- and nucleic acid-rich assemblies and lipid bilayers mutually remodel one another to generate specialized reaction environments. This mini-review focuses on two illustrative cases of membrane-associated condensates: remodelled cellular membranes that host viral replication assemblies and synaptic condensates that organize neurotransmitter release and engage disease-relevant proteins such as α-synuclein and Tau. Using these examples together with concepts derived from minimal reconstituted systems, the article outlines how condensate-membrane coupling can drive membrane remodelling and shape the formation and maintenance of these specialized phases. It then considers how this interfacial view opens opportunities for therapeutic intervention, positioning membrane-proximal condensates and their surrounding lipid environment as a distinct, potentially druggable space.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1808825</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1808825</link>
        <title><![CDATA[Linker peptide acts as an external mechanical clamp in a designed polyprotein]]></title>
        <pubdate>2026-05-04T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Yanwei Wang</author><author>Bin Zheng</author><author>Peng Zheng</author>
        <description><![CDATA[Rational protein design has successfully enhanced the mechanical stability of biomaterials by optimizing the internal topology of force-bearing domains. However, current design strategies predominantly focus on isolated monomers, paying less attention to the immediate oligomeric environment, such as the connecting linkers, modulates mechanical resistance. Here, we report a “Neighbor Peptide Effect” in SuperMyo A339, a recently de novo designed mechanostable protein with an engineered shear topology. Using single-molecule force spectroscopy, we demonstrate that oligomerization via a specific flexible linker (RSGGS) amplifies mechanical stability (∼15%), elevating the unfolding force from ∼350 pN in the monomer to ∼400 pN in the tetramers. Steered molecular dynamics simulations, together with contact-occupancy analysis, elucidate the molecular mechanism underlying this enhancement, revealing a discrete, sequence-specific interaction between the linker and the force-bearing loop of the adjacent domain. Specifically, an interfacial hydrogen bond between linker residue Ser117 and domain residue Lys218, which exhibits a 0.21 occupancy increase at the transition state, acts as an external mechanical clamp. This interaction may restrict loop stochasticity, optimize the pulling geometry and stabilize the core hydrogen-bond network, raising the energy barrier for unfolding without altering the protein’s core fold. These findings indicate that interfacial peptide design may serve as an external means to adjust the mechanical properties of protein.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1773451</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1773451</link>
        <title><![CDATA[Novel therapeutic approaches targeting biomechanical pathway alterations in bone diseases]]></title>
        <pubdate>2026-04-01T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Malkiet Kaur</author><author>Manju Nagpal</author>
        <description><![CDATA[Bone is a living tissue that undergoes continuous remodelling. This process is regulated not only by hormones and nutrients but also by biomechanical forces such as load, pressure, strain, and stress. These forces are sensed through molecular pathways in a process known as mechanotransduction. Osteocytes act as the main mechanosensors, triggering pathways including integrins, Wnt/β-catenin, ion channels, and prostaglandins. Their activation increases osteoblast activity and reduces osteoclast-mediated bone resorption, helping to maintain skeletal strength and integrity. When these biomechanical pathways are disrupted, bone diseases such as osteoporosis, osteoarthritis, etc., can develop. Current treatments rely largely on anti-resorptive and anabolic drugs, which improve bone turnover but do not correct the underlying mechanosensory defects. This makes targeting biomechanical pathways an exciting and novel therapeutic direction that could provide more effective and longer-lasting results. This review will explore how biomechanical regulation shapes bone biology, the consequences of altered mechanotransduction, and the recent advances in therapies designed to harness or restore these pathways. By drawing together knowledge from molecular biology, biomechanics, and clinical research, it aims to offer a broader perspective on improving bone disease management beyond traditional treatment approaches.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1795884</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1795884</link>
        <title><![CDATA[From the classical colloidal theory to biomolecular condensation: implications in health and disease]]></title>
        <pubdate>2026-03-25T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Noelia A. Melian</author><author>Aldana Gomez</author><author>Milagros B. Abate</author><author>Pamela L. Toledo</author><author>Mario R. Ermácora</author><author>Diego S. Vazquez</author>
        <description><![CDATA[Biomolecular phase separation and condensation are fundamental mechanisms of cellular compartmentalization that regulate biochemical processes in space and time. From a biophysical standpoint, biomolecular condensates can be considered biological colloids that share key properties with classical colloidal systems. In this article, we integrate classical colloidal theory with recent advances in biomolecular condensation to exemplify how physicochemical parameters, including pH, ionic strength, metal ions, and post-translational modifications, modulate the assembly dynamics and material properties of biomolecular condensates under physiological and pathological conditions. Additionally, we highlight the relationship between phase separation and amyloid formation, emphasizing recent evidence that amyloid-promoting proteins can exhibit catalytic activity in condensed or aggregated states. This perspective redefines biomolecular condensation and amyloid formation as highly versatile processes with significant implications for cell biology, disease mechanisms, and therapies.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2026.1804302</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2026.1804302</link>
        <title><![CDATA[IDRs in Cross-Membrane Transport: Regulation of Ion Channels and Transporters, Mechanistic Studies Made Possible by NMR and Computational Methods]]></title>
        <pubdate>2026-03-09T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Olga Vinogradova</author>
        <description><![CDATA[The roles of intrinsically disordered proteins (IDPs) and regions (IDRs) in health and disease have gained increasing attention in recent years. Understanding their structure–activity relationships remains challenging, especially for integral membrane proteins. This manuscript reviews current knowledge on IDR functions in cross-membrane transport, with a focus on ion channels and transporters. It also examines how NMR and computational methods can provide atomic-level mechanistic insights into cross-membrane transport and link these findings to the roles of disorder in this process.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1710099</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1710099</link>
        <title><![CDATA[Functional study of a novel SCN4A variant c.611C>T identified in a Japanese patient with myasthenia]]></title>
        <pubdate>2026-01-08T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Natsuki Kira</author><author>Kosuke Yoshida</author><author>Satoe Takahashi</author><author>Ayami Yamanaka</author><author>Takashi Kimura</author><author>Kazuaki Homma</author><author>Masanori P. Takahashi</author><author>Tomoya Kubota</author>
        <description><![CDATA[Recent advances in sequencing technologies have significantly contributed to the identification of disease-associated gene variants. However, a substantial number of patients, particularly those presenting with atypical neuromuscular phenotypes, remain genetically undiagnosed. Herein, we report a case of a Japanese patient with myasthenic symptoms in the eyelids and limbs rather than periodic paralysis having a novel heterozygous variant (c.611C>T) located at the 3′ end of exon 4 in SCN4A. The analysis of the proband’s SCN4A mRNA showed that this variant causes an alanine-to-valine missense change at the amino acid position of 204 (p.A204V, 39%) and a disruption of the splicing of exons 4 and 5 leading to the production of truncated Nav1.4 variant protein (p.A204Vfs*94, 4%). We anticipated that the p.A204V missense change would impair Nav1.4 function; however, the ion channel activity and membrane targeting of p.A204V Nav1.4 were found to be wild-type (WT)-like. We also examined the cytotoxicities of the p.A204V and p.A204Vfs*94 variants; however, the cell lines heterologously overexpressing these Nav1.4 variant proteins did not induce cell death any more than the WT control. Although the loss or gain of anomalous ion channel function that is commonly suspected in channelopathies was ruled out in the present case, the precise mechanism of the pathogenic role of c.611C>T SCN4A remains to be elucidated.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1693360</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1693360</link>
        <title><![CDATA[A blurry view of fuzzy objects: on the roles of low-resolution structural techniques in discovery and early characterization of intrinsically disordered proteins]]></title>
        <pubdate>2025-12-03T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Vladimir N. Uversky</author>
        <description><![CDATA[The discovery of intrinsically disordered proteins (IDPs) (and, therefore, the establishment of the field of protein intrinsic disorder) was initially driven by low-resolution techniques, which overturned the established “lock-and-key” paradigm of structural biology by showing that some proteins exist as a dynamic conformational ensemble rather than a single fixed structure. Though unable to provide atomic-level detail offered by X-ray crystallography or NMR, these methods were the first to reveal that many functional proteins exist as a dynamic ensemble of conformations rather than a single fixed structure. Furthermore, these techniques highlighted a limitation of high-resolution methods such as X-ray crystallography, which often could not resolve disordered regions. Curiously, despite the fact that X-ray crystallography requires rigid, crystalized samples and portrays the proteins as aperiodic crystals, this technique provided some early hints of intrinsic disorder that came from the “missing residues” in X-ray structures. Ultimately, by identifying proteins that lacked stable structures, these initial experiments utilizing low-resolution techniques drove the development of advanced approaches, such as specialized NMR techniques, to better characterize the dynamics of these proteins. The goal of this review is to emphasize the roles of low-resolution structural techniques in establishing the IDP field by showing some illustrative examples of IDPs they helped to discover in the years preceding the formal acceptance of the protein intrinsic disorder concept.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1693508</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1693508</link>
        <title><![CDATA[Vesicular and plasma membrane glutamate transporters]]></title>
        <pubdate>2025-10-30T00:00:00Z</pubdate>
        <category>Review</category>
        <author>Bart Borghans</author><author>Natalia Dmitrieva</author><author>Aleksandr Nikiforov</author><author>Christoph Fahlke</author>
        <description><![CDATA[Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. After exocytotic release from presynaptic nerve terminals, glutamate diffuses across the synaptic cleft and opens postsynaptic ionotropic glutamate receptors, thus depolarizing the postsynaptic neuron. Synaptic activity is terminated by rapid and efficient uptake into surrounding neurons and glial cells. The function of a glutamatergic synapse thus critically depends on two distinct transport systems: vesicular and plasma membrane glutamate transporters. Vesicular glutamate transporters (VGLUTs) accumulate glutamate in synaptic vesicles and determine the amount of released glutamate. Plasma membrane glutamate transporters (excitatory amino acid transporters, EAATs) clear the synaptic cleft from glutamate, setting the time resolution and energy demand of glutamatergic synaptic signaling. Both classes of glutamate transporters are not only secondary-active transporters, but also function as chloride channels, with different roles in chloride and glutamate homeostasis. Despite similar transport functions, VGLUTs and EAATs are structurally diverse and employ different molecular mechanisms to overcome the same chemical challenges. We here review recent progress in understanding the molecular and cellular biophysics of vesicular glutamate transporters and compare their properties with plasma membrane glutamate transporters.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1681011</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1681011</link>
        <title><![CDATA[Proton channel Hv1 modulates microglial responses to neurological disorders]]></title>
        <pubdate>2025-10-08T00:00:00Z</pubdate>
        <category>Mini Review</category>
        <author>Maite Stratmann</author><author>Caterina Gagliardi</author><author>Melania Capasso</author>
        <description><![CDATA[Proton channels are transmembrane proteins that enable selective proton (H+) transport. The voltage-gated proton channel Hv1 or HVCN1 is the only one found in mammalian cells, primarily in immune cells, where it facilitates rapid proton extrusion in response to membrane depolarization, mediating outward proton currents. Therefore, it is well equipped to support NADPH-oxidase function, facilitating the proton flux that maintains physiological pH and membrane potential for efficient reactive oxygen species (ROS) production. In the central nervous system (CNS), Hv1 is predominantly found in microglia. Its role in microglia homeostasis is yet to be elucidated; however, recent research has highlighted its involvement in neurological conditions, including demyelinating disease, spinal cord injury, stroke, and Parkinsonism. These studies have shown beneficial effects of Hv1 deletion, including improved neurological function, reduced microglial activation, enhanced myelination, and decreased neuroinflammation. This review explores the role of Hv1 in the CNS and its potential as a therapeutic target in neurodegenerative diseases.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1652466</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1652466</link>
        <title><![CDATA[Identification of voltage-gated calcium currents in Helix (Cornu) serotonergic neurons, subcellular localization, and role in calcium dynamics and cellular firing of CaV2.1 and CaV2.2 subtypes]]></title>
        <pubdate>2025-10-02T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>María Laura Ríos-Reyes</author><author>Silvia Calvo-Corea</author><author>Oscar Brenes</author>
        <description><![CDATA[Calcium not only contributes to changes in membrane potential but also acts as a central regulator of multiple cellular processes. Invertebrates have had a critical role throughout history as biological models for studying the nervous system at the cellular level due to the relative simplicity of their neural circuits and their high resistance to experimental manipulation. Among them, land snails of the genus Helix present the previously described characteristics while also being easy to maintain in the laboratory, and their neurons in culture reproduce in vitro their in vivo characteristics. However, the electrophysiological properties of their neurons remain incompletely characterized, and thoroughly understanding the biological model is essential to fully exploit its capabilities. To better characterize the ionic properties and distribution of the voltage-gated calcium channels (CaVs) in the serotonergic C1 neuron of Helix aspersa, we employed patch clamp recordings, calcium imaging and immunocytochemistry. Our results indicate that the C1 neuron exhibits exclusively high-voltage activated calcium currents and, according to the pharmacological dissection, these are mediated by CaV2.1 and CaV2.2-like channels. The CaV2.2-like channels were primarily localized in neurites, whereas functional varicosities, those expressing exocytic machinery, predominantly contain CaV2.1-like channels.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1648934</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1648934</link>
        <title><![CDATA[From biophysics to cellular function: neural TELCs-membrane-anions capacitor transmembrane potential]]></title>
        <pubdate>2025-09-18T00:00:00Z</pubdate>
        <category>Review</category>
        <author>James Weifu Lee</author>
        <description><![CDATA[Based on the transmembrane-electrostatically localized protons/cations charges (TELCs) theory, neural transmembrane potential including both resting and action potential is now well elucidated as the voltage contributed by the TELCs-membrane-anions capacitor biophysics in a neuron. Accordingly, neural transmembrane potential has an inverse relationship with TELCs surface density, which may represent a substantial progress in bettering the fundamental understanding of neuroscience. In this article, I will present a review on the latest development of the TELCs neural transmembrane potential theory and address Silverstein’s interesting arguments regarding the TELCs model that may constitute a complementary development to both the Hodgkin-Huxley classic cable theory and the Goldman-Hodgkin-Katz equation. A series of predictions from the TELCs model regarding crucial ion channels have exactly been experimentally observed in many well-established electrophysiological phenomena including (but not limited to): 1) The tetrodotoxin (TTX) sensitivity shows the complete blockade of action potentials by TTX; 2) Genetic knockout or mutation of critical ion channels abolishes action potential spike; and 3) The precise clustering of ion channels at the axonal initial segment and nodes of Ranvier underlies the ability to fire action potential spikes and the saltatory conduction along a myelinated axon. This indicates that the TELCs model can be well predictive and provide new opportunities as a theoretical tool for further research to better understand neurosciences.]]></description>
      </item><item>
        <guid isPermaLink="true">https://www.frontiersin.org/articles/10.3389/frbis.2025.1623880</guid>
        <link>https://www.frontiersin.org/articles/10.3389/frbis.2025.1623880</link>
        <title><![CDATA[Nanotribology of viruses reveals their adhesion strength and modality of motion on surfaces]]></title>
        <pubdate>2025-08-07T00:00:00Z</pubdate>
        <category>Original Research</category>
        <author>Charles Ault</author><author>Claudia Simon</author><author>Irina B. Tsvetkova</author><author>Pedro J. De Pablo</author><author>Bogdan Dragnea</author>
        <description><![CDATA[Virus adsorption at solid-water interfaces is an ubiquitous phenomenon in the lifecycle of waterborne viruses, both in natural environments and in engineered systems. Airborne aqueous microdroplets containing viruses readily attach to solid surfaces. Inside the droplet, viruses may adhere to the solid-liquid interface. Investigating virus adsorption at solid-water interfaces could lead to new ways to suppress virus infectivity. To further improve our understanding of virus adsorption, we studied the friction dynamics of icosahedral viruses adsorbed to solid surfaces. Using the lateral torsion of cantilevers in atomic force microscopy to move individual capsids in a liquid environment, we found that the virions tend to roll rather than slide on the surface. In contrast, rigid, ligand-stabilized gold nanoparticles are more likely to combine rolling with sliding under the same conditions. The experiments indicate that the force required to drag the viruses on the surface is four times less than that of AuNPs, while the lateral force work needed to induce virus movement was ∼104 kT, ten times less than that of the rigid gold nanoparticles. These results go beyond the paradigm that adhesion of nanoparticles is mainly governed by geometrical factors, such as size and area of contact, highlighting the need to amend modeling approaches to account for mechanically-compliant tribological response of biologically derived nanoparticles.]]></description>
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