Biochimica et biophysica acta. Biomembranes最新文献

{"title":"Crotalicidin and NA-CATH-ATRA-1-ATRA-1 peptide-induced membrane disruption in human breast cancer cells","authors":"Vanessa Gallego-Londoño ,&nbsp;Gloria A. Santa-González ,&nbsp;Juan M. Giraldo-Lorza ,&nbsp;Mauricio Rojas ,&nbsp;G. Bea A. Wisman ,&nbsp;Steven de Jong ,&nbsp;Marcela Manrique-Moreno","doi":"10.1016/j.bbamem.2025.184429","DOIUrl":"10.1016/j.bbamem.2025.184429","url":null,"abstract":"<div><div>Cationic peptides offer a promising alternative for cancer treatment due to their ability to target cancer cells via standard membrane features, thereby overcoming intratumoral heterogeneity. This study investigates the cytotoxic activity and the membrane-disruptive effects of two snake venom-derived peptides, Crotalicidin (Ctn) and NA-CATH-ATRA-1-ATRA-1 (NA) in human breast cancer cells. Cell viability assays showed that both Ctn and NA significantly diminished the viability of MCF-7 and MDA-MB-231 cells, with NA showing greater potency, as indicated by lower IC₅₀ values of 13.4 μM for MCF-7 and 6.4 μM for MDA-MB-231. Microscopy and flow cytometry revealed size reduction and increased granularity in treated cells. Further analyses indicated that the peptides induced membrane permeabilization, as evidenced by significant propidium iodide uptake, without significantly altering mitochondrial membrane potential. Apoptosis markers such as cleaved caspase-9 and PARP, were not detected by western blot.</div><div>Additionally, LDH release and confocal microscopic analysis supported the findings of membrane disruption. Finally, infrared spectroscopy (FT-IR) on lipid extracts revealed peptide-membrane interactions, resulting in phase transitions consistent with membrane disruption. These findings highlight the potent cytotoxic effects of Ctn and NA on breast cancer cells and their potential as novel therapeutic agents.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184429"},"PeriodicalIF":2.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144257297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Interaction of lensoside Aβ with lipids and proteins of HeLa cells","authors":"Justyna Kapral-Piotrowska ,&nbsp;Agata Wawrzyniak ,&nbsp;Jarosław Pawelec ,&nbsp;Barbara Zarzyka ,&nbsp;Roman Paduch ,&nbsp;Jerzy Żuchowski ,&nbsp;Adrianna Sławińska-Brych ,&nbsp;Barbara Zdzisińska ,&nbsp;Bartłomiej Pawlęga ,&nbsp;Alicja Wójcik-Załuska ,&nbsp;Ewa Baranowska-Wójcik ,&nbsp;Joanna Jakubowicz-Gil ,&nbsp;Wiesław I. Gruszecki ,&nbsp;Bożena Pawlikowska-Pawlęga","doi":"10.1016/j.bbamem.2025.184431","DOIUrl":"10.1016/j.bbamem.2025.184431","url":null,"abstract":"<div><div>Lensoside Aβ (LAβ) is a quercetin derivative isolated from the leaves and stems of the <em>Lens culinaris</em> cultivar Tina. Flavonoid-membrane interactions are crucial for their physiological and pharmacological activity. We have demonstrated the impact of LAβ on EYPC liposomes resembling the lipid phase of tumor cell membranes with the use of the ¹H NMR technique and have examined its activity on HeLa cells for the first time. To study the interactions of the tested compound with lipids and proteins at the molecular level, the FTIR technique was applied. To reveal changes in morphology and ultrastructure as well as examine its effect on apoptosis induction and cell viability, SEM, TEM, light, and fluorescence microscopy, flow cytometry analysis, LIVE/DEAD assays were employed. The ability of LAβ to induce oxidative stress was determined by staining with DHR123. The FTIR analyses indicated that LAβ interacts with the PO₂₋ groups in the polar head region. Moreover, a decrease in the relative protein concentration and changes in protein spectral profile in the amide I region were noted. Flavonoid reduced the viability of HeLa cells, which was correlated with the induction of apoptosis supported by SEM and TEM observations. Moreover, the addition of lensoside Aβ induced oxidative stress. These results confirm that lensoside Aβ may be used in novel therapeutic approaches for treating cervical cancer.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184431"},"PeriodicalIF":2.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144330690","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Amyloid-liposome composites as hybrid platforms for doxorubicin delivery","authors":"Valeriya Trusova,&nbsp;Uliana Malovytsia,&nbsp;Kateryna Vus,&nbsp;Olga Zhytniakivska,&nbsp;Galyna Gorbenko","doi":"10.1016/j.bbamem.2025.184426","DOIUrl":"10.1016/j.bbamem.2025.184426","url":null,"abstract":"<div><div>The feasibility of engineering the sophisticated hybrid drug delivery platforms through the integration of phospholipid vesicles within a matrix of amyloid suspensions has been evaluated. Utilizing the equilibrium dialysis methodology and spectrofluorometric technique, the quantitative analysis of doxorubicin (DOX) encapsulation capacity of diverse phospholipid assemblies, amyloid suspensions, and their corresponding composite systems has been performed. Our findings revealed that the incorporation of negatively charged cardiolipin (CL) into phosphatidylcholine (PC) lipid vesicles significantly enhances DOX encapsulation and retention, while the addition of amyloid fibrils to charged liposomes has minimal impact on the drug binding. The neutral PC liposomes modified with insulin and lysozyme fibrillar suspensions exhibited improved doxorubicin encapsulation and retention compared to unmodified liposomes, thereby displaying a potential for reduced toxicity and prolonged drug action <em>in vivo</em>. Notably, amyloid fibrils alone were found to demonstrate the lower degree of DOX encapsulation and retention as compared to liposomes. Fluorimetric analysis suggests that the presence of insulin and lysozyme fibrils alters the microenvironment of DOX towards a more hydrophobic which is consistent with deeper bilayer penetration. Cumulative data from release kinetics and retention studies along with fluorescence measurements suggest that PC liposome-insulin fibril composites represent the most promising DOX nanocarriers, combining enhanced drug encapsulation, structural stability, and optimal drug location within the bilayer. The results obtained provide valuable insights into the design of protein-lipid nanomaterials for enhanced drug delivery, offering promising avenues for the development of more effective and targeted therapeutic strategies.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184426"},"PeriodicalIF":2.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144130922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Membrane properties control the ATPase activity of the ABC transporter BmrA","authors":"Veronika Osten ,&nbsp;Dirk Schneider","doi":"10.1016/j.bbamem.2025.184430","DOIUrl":"10.1016/j.bbamem.2025.184430","url":null,"abstract":"<div><div>The structure and the function of membrane proteins can be affected by the lipid bilayer environment, yet its impact is often neglected in <em>in vitro</em> studies where proteins are typically analyzed in membrane mimetics, mostly liposomal systems. It has been observed that the activity of the bacterial ATP-binding cassette (ABC) transporter BmrA (<em>Bacillus</em> multidrug resistance ATP) differs when measured in detergent <em>vs.</em> a model membrane environment, indicating that the physico-chemical properties of the membrane environment crucially affect the protein's activity. We now performed a systematic analysis to elucidate the impact of individual lipid/membrane properties on the activity of BmrA and identified three parameters controlling the BmrA activity in lipid bilayers: (i) the hydrophobic thickness of the membrane, (ii) a negative surface charge, and (iii) the packing of lipids in the acyl-chain and head group regions. Our study provides valuable insights into how a specific lipid composition can influence the basal ATPase activity of BmrA and emphasizes that the lipid composition should be carefully selected in <em>in vitro</em> studies of membrane proteins.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 5","pages":"Article 184430"},"PeriodicalIF":2.8,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144322078","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Elucidating the interactions of endocannabinoid-like neurotransmitters, N-acyltaurines and bovine serum albumin: Spectroscopic and computational approaches","authors":"Martin Luther John ,&nbsp;Sivaramakrishna Akella ,&nbsp;Ravi Kanth Kamlekar","doi":"10.1016/j.bbamem.2025.184421","DOIUrl":"10.1016/j.bbamem.2025.184421","url":null,"abstract":"<div><div><em>N</em>-Acyltaurines (NATs) are endogenous neurotransmitters, structurally similar to endocannabinoids, and have anti-inflammatory and anti-proliferative effects. In response to NATs, TRP channels, TRPV1, TRPV4 and the peptide hormone, GLP-1 are activated. Serum albumin proteins act as transporters for a variety of substances in blood plasma (i.e., hormones, fatty acids, bilirubin, ions, and medications). Due to the structural closeness of Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA), a study into NAT-BSA interactions is crucial. To study interactions of NATs (<em>n</em> = 10–18) with BSA, spectroscopic and computational techniques were used. From the steady-state fluorescence measurements, observed binding constants are in the range of 1.57 × 10⁵ M⁻¹ to 2.85 × 10⁵ M⁻¹. Due to the binding of NATs, the fluorescence of BSA is quenched (∼24.77 %). The negative enthalpy and entropy change and Gibbs free energy values, obtained from van't Hoff plot indicate that the interactions between NATs and BSA are spontaneous and primarily driven by hydrogen bonding. Competitive site-binding assays with warfarin and ibuprofen show that NATs bind to both the drug-binding sites in BSA concurrently. The CD spectroscopic and FT-IR analysis indicates relatively marginal changes in the secondary structure of BSA. Molecular docking analyses are done to identify binding locations and molecular-level interactions. The negative free energy values indicate that NATs have a positive binding relationship with BSA. These findings are congruent with the findings of site-binding studies, which reveal that NATs have a higher proclivity for interacting with sites I and II at the same time.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184421"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143844050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of osmolytes on the conformational stability of Aβ(25–35): A circular dichroism analysis","authors":"Angelo Santoro ,&nbsp;Michela Buonocore ,&nbsp;Anna Maria D'Ursi","doi":"10.1016/j.bbamem.2025.184420","DOIUrl":"10.1016/j.bbamem.2025.184420","url":null,"abstract":"<div><div>Alzheimer's (AD) is a neurodegenerative disease characterized by the onset and progression of mental decline. AD aetiopathogenesis is still questioned; however, according to one of the most accredited hypotheses, the accumulation of amyloid plaques formed by aggregated Aβ peptides is the primary cause of neuronal function loss. Accordingly, hundreds of molecules have been screened for their possible action to prevent or destroy amyloid aggregates. Following this track, osmolytes, naturally occurring small molecules produced by several organisms in response to external stressors, were recently evaluated as modulators of Aβ aggregation. In this study, we examined the conformational stability of Aβ(25–35) when exposed to the osmolytes acetylcholine (ACh), succinylcholine (SCh), and betaine (Bet). Aβ(25–35) is the shortest fragment known for replicating the aggregation process seen in Aβ peptides. By collecting circular dichroism (CD) spectra in water and different membrane-mimicking systems, we investigated the potential of the mentioned osmolytes to stabilize the soluble conformations of Aβ(25–35) and preserve them from denaturing conditions. Our data suggest that Bet is a promising small molecule that can safeguard the soluble form of Aβ peptide and is effective in counteracting environmental conditions by favoring the amyloid aggregation associated with pathology progression.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184420"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787660","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Structural analysis of the NK-lysin-derived peptide NK-2 upon interaction with bacterial membrane mimetics consisting of phosphatidylethanolamine and phosphatidylglycerol” [BBA – Biomembr. 1866 (2024) 184267]","authors":"Jörg Andrä ,&nbsp;Christopher Aisenbrey ,&nbsp;U.S. Sudheendra ,&nbsp;Marc Prudhon ,&nbsp;Gerald Brezesinski ,&nbsp;Evgeniy S. Salnikov ,&nbsp;Claudia Zschech ,&nbsp;Regine Willumeit-Römer ,&nbsp;Matthias Leippe ,&nbsp;Thomas Gutsmann ,&nbsp;Burkhard Bechinger","doi":"10.1016/j.bbamem.2025.184416","DOIUrl":"10.1016/j.bbamem.2025.184416","url":null,"abstract":"","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184416"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143381577","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Long-chain cationic gemini surfactants as drug retention adjuvant on liposomes. A methodological approach with atorvastatin","authors":"Yago Radziunas-Salinas ,&nbsp;Vicente Domínguez-Arca ,&nbsp;Alberto Pardo ,&nbsp;Adriana Cambón ,&nbsp;Pablo Taboada ,&nbsp;Gerardo Prieto","doi":"10.1016/j.bbamem.2025.184419","DOIUrl":"10.1016/j.bbamem.2025.184419","url":null,"abstract":"<div><div>This study delves into the development and characterization of dipalmitoyl phosphatidylcholine (DPPC) liposomes incorporated with gemini surfactant (tetradecamethylene-1,14 bis(dimethyl tetradecyl ammonium bromide); 14-14-14) and atorvastatin, aimed at enhancing drug delivery efficiency for cardiovascular diseases. The integration of gemini surfactants into liposomes is investigated for its potential to improve atorvastatin encapsulation and retention, addressing the drug's poor water solubility and the limitations of conventional liposomal systems. Through a combination of dynamic light scattering (DLS), differential scanning calorimetry (DSC), and molecular dynamics (MD) simulations, the study reveals that the presence of gemini surfactants significantly reduces liposome size and polydispersity, indicative of a more uniform and potentially unilamellar structure. DSC analysis highlights a decrease in transition temperatures and an alteration in transition symmetry, suggesting enhanced stability and a favourable drug release profile at physiological temperatures. MD simulations provide insight into the internalization mechanism of gemini surfactants and atorvastatin within the liposomal bilayer, demonstrating their mutual incorporation facilitated by polar interactions. Spectrophotometry-based retention studies further confirmed that liposomes containing gemini surfactants exhibit superior atorvastatin retention capabilities, nearly doubling the encapsulation efficiency compared to conventional liposomes. This research highlights the promising role of gemini surfactant-incorporated liposomes as an efficient drug delivery platform for cardiovascular therapeutics, offering insights into the molecular interactions and structural dynamics underlying their enhanced performance.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 4","pages":"Article 184419"},"PeriodicalIF":2.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143787602","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Differential insertion of arginine in saturated and unsaturated lipid vesicles","authors":"Hugo A. Perez,&nbsp;María A. Brandan,&nbsp;Aníbal Disalvo,&nbsp;María de los A. Frías","doi":"10.1016/j.bbamem.2024.184405","DOIUrl":"10.1016/j.bbamem.2024.184405","url":null,"abstract":"<div><div>In this work, the effects of L- Arginine (L-Arg) insertion on saturated and unsaturated lipid membranes were assessed by fluorescence spectroscopy, dynamic light scattering (DLS) and monolayer measurements. The studied systems were composed by DPPC, 16:0 DietherPC, 16:1 Δ9-CisPC, DPPC:Chol, 16:1 Δ9-CisPC:Chol, and 16:1 Δ9-CisPC:DPPC in the presence of increasing concentrations of L-Arg.</div><div>The information obtained using fluorescence spectral Laurdan properties indicates that L- Arg produces a decrease in the polarizability of saturated lipids congruent with the increase in vesicle size and area per lipid. However, in unsaturated lipids, the polarizability increases without significant changes in size and area per lipid denoting a different mechanism of insertion. The two opposite effects can be modulated by the saturated and unsaturated ratio and are independent of carbonyl groups. This modulation is damped by cholesterol. The differences in the L-Arg insertion can be explained considering that in the presence of the double bonds, L-Arg decreases the organized water in the lipid matrix without expanding the bilayer. Instead, in saturated lipid membranes, L-Arg inserts into the acyl chains dragging water and expanding the membrane area.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 3","pages":"Article 184405"},"PeriodicalIF":2.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142871178","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Replacement of phenyl substituents at phosphorus by hexyl ones in 2-(2-hydroxyaryl)vinylphosphonium salts can tune the nature of the induced proton transport through lipid membranes","authors":"Tatyana I. Rokitskaya ,&nbsp;Ljudmila S. Khailova ,&nbsp;Anna G. Strelnik ,&nbsp;Elena A. Kotova ,&nbsp;Vladimir F. Mironov ,&nbsp;Dmitry A. Tatarinov ,&nbsp;Yuri N. Antonenko","doi":"10.1016/j.bbamem.2025.184417","DOIUrl":"10.1016/j.bbamem.2025.184417","url":null,"abstract":"<div><div>2-(2-hydroxyaryl)vinylphosphonium salts are zwitterionic protonophores previously shown to induce proton transport across lipid membranes via cyclic deprotonation and protonation of the hydroxyl group. Here, we examine the impact of the kind of substituents at phosphorus on the protonophoric activity of these compounds. In particular, replacement of all the three phenyl groups at the phosphorus atom of the 2-(2-hydroxyaryl)vinyl(triphenyl)phosphonium salt (<strong>2HVPPh</strong>_{<strong>3</strong>}) by hexyl chains (<strong>2HVPHex</strong>_{<strong>3</strong>}) led to a tremendous increase in electric current induced by the phosphonium salt across planar bilayer lipid membranes (BLM). Remarkably, the BLM conductance quadratically increased with increasing <strong>2HVPHex</strong>_{<strong>3</strong>} concentration, whereas a linear concentration dependence of the BLM current was observed for <strong>2HVPPh</strong>_{<strong>3</strong>}, <strong>2HVPHexPh</strong>_{<strong>2</strong>} ((hexyl)diphenyl) and <strong>2HVPHex</strong>_{<strong>2</strong>}<strong>Ph</strong> ((dihexyl)phenyl), i.e., in the presence of at least one phenyl substituent at the phosphorus atom. Proton selectivity of the <strong>2HVPHex</strong>_{<strong>3</strong>}-induced electric current was close to perfect in membranes formed of diphytanylphosphatidylcholine with the decreased dipole potential, but rather low in membranes formed of the usual synthetic lipid – diphytanoylphosphatidylcholine. We hypothesize that the proton transport across BLM is carried out by <strong>2HVPHex</strong>_{<strong>3</strong>} dimers. By contrast, the uncoupling activity of <strong>2HVPHex</strong>_{<strong>3</strong>} in isolated rat liver mitochondria was observed at similar concentrations, as found for the compounds with phenyl substituents, thereby indicating that dimers do not play a key role in the uncoupling process. At the same time, the rate of <strong>2HVPHex</strong>_{<strong>3</strong>}-induced mitochondrial swelling under the deenergized conditions in potassium acetate medium, reflecting the protonophoric activity of the compound in mitochondria, significantly exceeded that for other compounds.</div></div>","PeriodicalId":8831,"journal":{"name":"Biochimica et biophysica acta. Biomembranes","volume":"1867 3","pages":"Article 184417"},"PeriodicalIF":2.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143453902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}