The Austrian Biophysical Society (Biophysics Austria) was founded in 1961, making it one of the oldest national biophysical societies in Europe. It hosted the first European Meeting in Biophysics in Baden near Vienna in 1971 and celebrated its 60th anniversary by hosting the 13th European Biophysics Congress in Vienna as a hybrid event during the COVID-19 pandemic in 2021. In 2026, the society is celebrating its 65th anniversary. This review reflects on the society´s history and highlights events, milestones, and people who have contributed to its development.

Bax-interacting factor-1 (BIF-1), also known as endophilin B1 (SH3GLB1), is a membrane-associated protein involved in apoptosis, autophagy, and membrane dynamics. There is growing evidence of a context-dependent role in tumor biology, mainly associated with tumor-suppressive functions in several cancers. In this narrative review, we summarize current evidence regarding BIF-1 expression patterns and its functional relevance in cancer-related pathways. Downregulation of BIF-1 has been consistently reported in melanoma, breast cancer, prostate cancer, gastric carcinoma, colorectal cancer, urinary bladder cancer and gallbladder cancer, where reduced expression is associated with impaired apoptosis, altered autophagy and tumor progression, supporting its potential value as a tumor suppressor-associated biomarker. On the other hand, hepatocellular carcinoma shows a context-dependent expression pattern and inconsistent associations with clinical outcomes. Its clinical utility in these tumors is limited because diagnostic and prognostic significance has not been consistently demonstrated. Therapeutic studies suggest that modulation of BIF-1-related pathways could influence autophagy, apoptosis and cellular metabolism, implying indirect participation in cancer treatment strategies. In general, BIF-1 seems to be a potential biomarker linked to tumor suppression in various epithelial cancers, especially in melanoma, breast, and prostate cancers. However, it's clinical utility remains limited or appears variable in pancreatic ductal adenocarcinoma and Merkel cell carcinoma. These findings highlight the context-dependent role of BIF-1 in tumor biology.

Focal adhesion (FA) dynamics and cell migration depend sensitively on the mechanical properties of the extracellular matrix, yet substrate stiffness alone cannot account for the distinct behaviours observed on natural versus artificial materials. In this review, we synthesize experimental findings on cells interacting with collagen I matrices and viscoelastic hydrogels, and identify the key physical mechanisms that govern adhesion stability, turnover, and migratory efficiency. Collagen I substrates are characterized by structural anisotropy, spatial heterogeneity, and a broad spectrum of relaxation times, in contrast to the simplified and often isotropic response of artificial hydrogels. Based on these observations, we highlight the central role of interfacial slippage at the FA-substrate biointerface enabled by matrix remodelling and multi-timescale viscoelastic dissipation. We further discuss how cell-generated forces can induce collagen reorganization and surface tension gradients, potentially driving Marangoni-like flows that contribute to dynamic matrix redistribution. These processes collectively maintain adhesions in a state between stabilization and turnover, favourable for persistent migration. Finally, we consider the interplay between these mechanical mechanisms and mechanosensitive signalling, particularly involving Piezo1 ion channels. This perspective emphasizes that effective cell-matrix coupling arises from the ability of the substrate to dissipate and reorganize distribution of mechanical energy, rather than from stiffness alone.

Electrical impedance sensing offers a powerful, non-invasive method for real-time monitoring of cellular behaviour; with applications spanning immunology, cancer biology and drug discovery. Adoption of impedance-sensing approaches has been accelerated by the commercial availability of the ECIS, xCELLigence, ScioSpec and cellZscope platforms; however, the complexity and volume of impedance datasets produced has limited rigorous analysis. vascr, an open-source R-based toolkit designed to streamline the processing of impedance sensing datasets was created to facilitate rapid and simplified handling of cellular impedance sensing data. vascr can import multi-frequency data from multiple instrument manufacturers and includes robust analysis tools for resampling, outlier detection, and statistical testing using ANOVA and cross-correlation. Using the vascr workflow, impedance sensing data can be rapidly and robustly interpreted, allowing for real-time investigation of the effects of biological agents on cellular processes such as endothelial barrier integrity.

Collagen deposition and alignment in the tumor stroma stiffen the extracellular matrix and, via integrin signaling, stimulate proton extrusion by cancer cells. In aggressive tumors, migration occurs preferentially along aligned collagen fibers, where proton efflux at the leading edge acidifies and degrades the matrix to facilitate invasion. Whether directional proton diffusion along collagen fibers exacerbates invasion remains uncertain, as it is not known how far protons can travel along a fiber before being released. To characterize the release barrier, we labeled collagen lysine side chains with a pH-sensitive fluorescein derivative and introduced an interfacial proton flux by microinjecting HCl near the surface of self-assembled collagen fibers elevated above the chamber bottom. Proton wave propagation was monitored by wide-field fluorescence microscopy. Quantitative analysis of the fluorescence transients revealed that proton migration is best described by a one-dimensional diffusion model with a finite surface-to-bulk release rate. A single global parameter set consistently described all experiments. From the fitted release rate, we determined a Gibbs activation energy barrier ΔG[‡] of approximately 30 kBT, comparable to values reported for membrane-water interfaces. These results demonstrate that protons can travel tens of micrometers along collagen fibers before equilibrating with the bulk solution, suggesting that membrane-anchored collagen fibers may provide an effective pathway for directing acidification along migration tracks in tumor stroma.

Folate biosynthesis is essential for the survival of bacteria and other lower organisms, yet absent in mammals, making its enzymes promising targets for selective antimicrobial therapy. Dihydropteroate synthase (DHPS) catalyzes a key step in this pathway by condensing para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPPP) to generate dihydropteroate. DHPS is also the cellular target of sulfonamide antibiotics, and the emergence of sulfonamide resistance underscores the need for detailed structural insights into substrate recognition and inhibitor design. Here, we report high-resolution crystal structures of Thermus thermophilus HB8 DHPS (TtDHPS) in its apo form (at 1.65 Å resolution) and in complex with pABA (at 1.9 Å resolution) and the pterin substrate analogue 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (6-HMPPP) (at 1.9 Å resolution). TtDHPS adopts a classical TIM-barrel fold and forms a biologically relevant dimer stabilized by C-terminal α-helices. Comparative analysis of the apo and ligand-bound forms reveals substrate-induced ordering of flexible loop regions that, together with residues from the barrel core, define the pterin- and pABA-binding pockets. Structural and sequence analyses with DHPS homologs from Escherichia coli and Mycobacterium tuberculosis highlight conserved catalytic features, as well as variable loop conformations and phosphate-binding residues that may contribute to differential sulfonamide sensitivity. Collectively, these structures shed light on DHPS catalysis and may prove helpful in the study of inhibitors associated with sulfonamide resistance.

Motivated by experimental observations that T-cells can activate as a consequence of clustering of T-cell receptors, we hypothesize that steric confinement between the intracellular chains of the TCR could play a role. Using coarse-grained simulations, we show that steric interactions between TCRs are sufficient to induce appreciable stretch of the intracellular domains of CD3ζ chains. We propose a model, in which the difference in membrane distances between the phosphatase CD45 and the kinases lck and fyn is able to sense the clustering-induced CD3ζ stretch: we estimate a 1.5- to 2-fold increase in phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) at CD3ζ upon TCR clustering.

The plasma membrane hosts a diverse set of proteins whose attachment, detachment, and lateral diffusion give rise to complex spatiotemporal patterns that regulate essential cellular processes. In motile eukaryotic cells, localized protein patterns at the membrane control actin organization and thereby establish a front-rear axis that drives locomotion. While persistent migration following a chemotactic signal can be captured by deterministic reaction-diffusion models coupled to a phase-field description of cell shape, amoeboid motion in cells such as neutrophils and Dictyostelium discoideum is markedly more irregular and requires the inclusion of stochastic effects. Existing modeling approaches typically introduce external noise into pattern-forming mechanisms or, alternatively, although much less frequently, they account for intrinsic fluctuations arising from the small number of participating molecules. Here, we compare and connect these two complementary modeling strategies for membrane protein dynamics driving cell locomotion in Dictyostelium discoideum. We present a stochastic reaction-diffusion model coupled to a phase field, previously calibrated to experimental data, alongside a related formulation in which fluctuations emerge intrinsically from molecular discreteness. Through systematic numerical simulations, we characterize the resulting membrane patterns and dynamical behaviors. Our results test the hypothesis that externally imposed fluctuations can be effectively reduced to intrinsic noise derived from first principles. We highlight the critical role of temporal correlation, a key feature of the original phenomenological formulation, and contrast it with the behavior of internal fluctuations. Finally, we discuss the relative strengths, differences, and physical limitations of both stochastic approaches.

Magnetite nanoparticles (MNPs, Fe3O4) have gained considerable interest for various biomedical applications. Gramicidin A (GrA) is a linear pentadecapeptide that plays an important role in modifying the biophysical and biological properties of membranes. Elucidating how GrA modulates the interaction between MNPs and biomembranes is essential for deepening our understanding of membrane biophysics and guiding the development of nanomedicine. We investigated the effects of GrA on anionic MNPs-induced deformation, membrane permeation, and the stability of cell-mimetic giant unilamellar vesicles (GUVs) under physiological conditions. The membranes of the GUVs were prepared using a combination of negatively charged lipid, neutral lipid, and varying GrA. The degree of deformation (e.g., compactness) decreased with increasing GrA. The leakage of encapsulated calcein from the GUVs indicated membrane poration caused by the adsorption of MNPs into the membranes. The leakage rate initially decreased and then increased as GrA rose. To assess membrane stability, we examined constant tension-induced rupture of GUVs by varying GrA using the micropipette technique. The rupture rate constant also showed a biphasic response, initially decreasing and then increasing with the increase of GrA at a constant membrane tension. Thus, GrA modulates the mechanical stability of membranes, along with MNPs-induced vesicle deformation and lipid membrane poration.

Protein arginine methyltransferases (PRMTs) catalyze arginine methylation, a key post-translational modification (PTM) regulating chromatin organization, RNA metabolism, and signaling. Recent studies reveal that PRMT-mediated methylation also modulates liquid-liquid phase separation (LLPS), which organizes membraneless condensates controlling transcription, stress response, and genome stability. Dysregulated PRMT activity disrupts condensate dynamics, contributing to cancer and neurodegenerative diseases. In cancer, PRMT1, PRMT5, and PRMT6 promote tumor progression via methylation-dependent condensates that enhance oncogenic transcription and stress resistance. In the nervous system, PRMT1, PRMT4, PRMT5, PRMT6, and PRMT8 regulate LLPS of proteins, linking aberrant methylation to ALS and Huntington's disease. This review highlights PRMTs as key modulators of phase separation and potential therapeutic targets in both oncology and neurodegeneration.

In the quantitative characterization of experimental systems the observation of a time-independent response can signify the attainment of thermodynamic equilibrium. However, there are also situations where the time-independence of experimental response merely reflects the attainment of a kinetic steady state. Although quantitative expressions derived on the basis of kinetic steady-state attainment retain validity for a system at thermodynamic equilibrium, those based on attainment of thermodynamic equilibrium do not apply to systems merely reflecting the attainment of a kinetic steady state. This survey of experimental procedures encountered during research endeavours over the past six decades has revealed many situations where the source of the time-independent instrumental response was correctly identified, but also a number where the responses were misinterpreted.

Red fluorescent protein mRuby is an important labelling tool for super-resolution imaging. With the addition of thioacetate, it was found here that the red colour of the protein aqueous solution changed, although still clear and transparent. Light spectrophotometry exhibited that, with the increase of thioacetate concentration, the absorption spectra changed abruptly. Crystallography showed the binding of thioacetate at the chromophore of mRuby. Atomic-resolution serial structures of mRuby single crystal showed snapshots of step-by-step reduction of thioacetate upon light irradiation. This observation suggests new insights for FP-compound interaction research and light energy harvesting for green chemistry.

The article presents a study on the disruption of the bacterial membrane by celandine (CME) and dandelion (TOE) extracts containing bioactive compounds responsible for their antibacterial activity. The in vitro microbiological tests showed antibacterial effect both on Gram-positive (Staphylococcus aureus and Streptococcus pyogenes) and Gram-negative (Escherichia coli and Pseudomonas aeruginosa) pathogenic bacteria species. However, in the case of celandine herb extract, the effect was stronger, especially for Gram-positive bacteria. For a deeper understanding of the mechanism of antibacterial action, both studied extracts were subjected to biophysical studies on artificial bacterial lipid membranes, modeled with the Langmuir monolayers technique. The monolayer investigations were performed using two approaches: (i) monitoring the penetration of extracts injected into the aqueous subphase beneath a compressed lipid film, and (ii) comparing surface pressure-area isotherms recorded on a subphase with and without addition of extracts. These experiments confirmed the activity of TOE and CME at the membrane level, demonstrating the penetration of extract components into the membranes and their fluidizing effect. AFM analysis of the domain structures of the films transferred onto solid supports (Langmuir-Blodgett) revealed differences in film topography induced by the extracts and are in a good agreement with the results of biological tests and analytical analyses of the tested extracts. These findings confirm that the stronger antibacterial effect of CME, associated with a higher content of bioactive compounds, exerts a more destructive effect on the bacterial lipid membranes compared to TOE.

Advances in artificial intelligence, particularly in deep learning, are transforming the field of protein structure prediction. AlphaFold has emerged as a benchmark tool due to its remarkable ability to model protein folding based solely on amino acid sequences. Nevertheless, despite these impressive achievements, several prediction failures still occur. In this study, we focus on two multidomain proteins, LicT from Bacillus subtilis and P1 from the Rice Yellow Mottle Virus, that have long resisted structural characterization. Both proteins exhibit inter-domain flexibility, dimerization, and dynamic behavior in response to phosphorylation (for LicT) or zinc binding (for P1). Here, we screen the performances of AlphaFold versions against these two proteins endowed with a complex conformational landscape and show the present impossibility to correctly predict all domains simultaneously.

A quick, noninvasive method based on [31]P NMR spectroscopy to measure the pH of samples containing phosphate buffer is presented. By taking advantage of all four phosphate species populated at acidic, mildly acidic, mildly alkaline and alkaline pH, the method is applicable over a wide range of pH values, from 1 to 13. This tool is most precise at pH values near the pKa values, namely from 5.8 to 8.0 and 10.6 to 13.0. To facilitate its use, a web application is presented that calculates the pH value directly from phosphate [31]P chemical shift (ppm) when sodium or potassium is the cation: (https://rmni.iqf.csic.es/software/31phnmr/). In addition, the potential of this approach to monitor reactions which generate or consume H[+] is illustrated by following the hydrolysis of GTP catalyzed by Ras-like protein in brain 1a (Rab1a), an essential protein linked to Parkinson's disease and tuberculosis. The intrinsic GTPase rate of Rab1a is found to be 3.3 ± 0.8·10[- 3] min at 37 °C, which places Rab1a amoung the Rabs with slow GTPase rates and the longer lived "active" GTP-bound states.