Biophysical chemistry最新文献

{"title":"Fifty-hertz magnetic fields induce DNA damage through activating mPTP associated mitochondrial permeability transition in senescent human fetal lung fibroblasts","authors":"Chuan Sun ,&nbsp;Sanying Wang ,&nbsp;Jing Zhang ,&nbsp;Xuqiang Zhou ,&nbsp;Tianjun Zhu ,&nbsp;Genxiang Mao","doi":"10.1016/j.bpc.2024.107367","DOIUrl":"10.1016/j.bpc.2024.107367","url":null,"abstract":"<div><div>With the rapid development and using of electromagnetic technology, artificial electromagnetic fields (EMFs) have become an emerging environmental factor in our daily life. Extremely-low-frequency (ELF) magnetic fields (MFs), generally generated by power lines and various electric equipment, is one of the most common EMFs in the environment which were concerned for the potential impact on human health. Base on limited evidence, ELF-MFs have been classified as possible carcinogen to human by International Agency for Research on Cancer (IARC), but the mechanisms have not been fully elucidated. Senescent cells are a group of special cells, characterized by cell cycle arrest, senescence-associated secretory phenotype (SASP), accumulation of macromolecular damage, and metabolic disturbance, play important role in fetal development, tissue aging, and even carcinogenesis. Thus, EMFs may promote carcinogenesis by affecting senescent cells, however, there are few studies. In this study, we found that exposure to 50 Hz MFs at 1.0 mT for 24 h could induce significant DNA damage in senescent but not non-senescent human fetal lung fibroblast suggested that senescent cells are more sensitive to 50 Hz MFs on DNA damage, and further results revealed that reactive oxygen species (ROS) generation mediated by mitochondrial permeability transition pore (mPTP) activation play critical role in this process. Our results indicated that cellular senescence can lead to cell sensitivity to the DNA damage effect of 50 Hz MFs, however, whether this play important role in mediating the carcinogenesis of EMFs await further study.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"318 ","pages":"Article 107367"},"PeriodicalIF":3.3,"publicationDate":"2024-12-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142790612","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":"Trp residues near peptide termini enhance the membranolytic activity of cationic amphipathic α-helices","authors":"Erik Strandberg ,&nbsp;Patrick Horten ,&nbsp;David Bentz ,&nbsp;Parvesh Wadhwani ,&nbsp;Jochen Bürck ,&nbsp;Anne S. Ulrich","doi":"10.1016/j.bpc.2024.107365","DOIUrl":"10.1016/j.bpc.2024.107365","url":null,"abstract":"<div><div>KIA peptides were designed as a series of cationic antimicrobial agents of different lengths, based on the repetitive motif [KIAGKIA]. As amphiphilic helices, they tend to bind initially to the surface of lipid membranes. Depending on the conditions, they are proposed to flip, insert and form toroidal pores, such that the peptides are aligned in a transmembrane orientation. Tryptophan residues are often found near the ends of transmembrane helices, anchoring them to the amphiphilic bilayer interfaces. Hence, we introduced Trp residues near one or both termini of KIA peptides with lengths of 14–24 amino acids. Our hypothesis was that if Trp residues can stabilize the transmembrane orientation, then these KIA peptides will exhibit an increased propensity to form pores, with increased membranolytic activity. Using solid-state ¹⁵N NMR, we found that peptides with Trp near the ends are indeed more likely to be flipped into a transmembrane orientation, especially short peptides. Short KIA peptides also exhibited higher antimicrobial activity when modified with Trp, while longer peptides showed similar activities with and without Trp. The hemolytic activity of KIA peptides of all lengths was higher with Trp near the ends. Vesicle leakage was also increased (sometimes more than 10-fold) for the Trp-mutants, especially in thicker membranes. Higher functionality of amphiphilic helices may thus be achieved in general by exploiting the anchoring effect of Trp. These results demonstrate that the incorporation of Trp increases membranolytic activities (vesicle leakage, hemolysis and antimicrobial activity), in a way compatible with a transmembrane pore model of peptide activity.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"318 ","pages":"Article 107365"},"PeriodicalIF":3.3,"publicationDate":"2024-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142806077","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":"The swelling behaviour of hair studied through the structural change of keratin protein during the permanent waving treatment","authors":"Takayuki Togashi ,&nbsp;Maako Tabata ,&nbsp;Akimasa Mochizuki ,&nbsp;Jiro Tanaka ,&nbsp;Kaori Wada ,&nbsp;Yoshio Muroga ,&nbsp;Hiroki Ikake","doi":"10.1016/j.bpc.2024.107364","DOIUrl":"10.1016/j.bpc.2024.107364","url":null,"abstract":"<div><div>Filament of human hair is formed from <em>α</em>-keratin protein and its physical property is predominantly dominated by the structure of microfibril (also known as intermediate filaments (IF)). It is known that human hair is swollen by permanent waving (pw) treatment which consists of the reducing process and following oxidizing process, but a detail in the swelling behaviour remains still unclarified. The present work was devoted to the analysis of the swelling behaviour of hair through the structural change of IF during pw treatment, where 1.0 mol/L ammonium thioglycolate solution (pH 9.25) was employed as reducing reagent. The structure of IF was represented in terms of its microstructure, which is given by <em>α</em>-helix content in keratin chain, and its macrostructure, which is given by alignment of IF along human hair axis, and the structures were studied by SAXS and CP/MAS ¹³C NMR and others. It is shown that the microstructure and macrostructure of IF simultaneously start to change at an initial stage of the pw treatment without any induction period and both structures are sufficiently swollen at that stage. Furthermore, it is shown that the microstructure and macrostructure of IF is partly destructed by reducing treatment, but the destructed structures are considerably restored by following oxidizing treatment.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"318 ","pages":"Article 107364"},"PeriodicalIF":3.3,"publicationDate":"2024-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142790948","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":"ROC-guided virtual screening, molecular dynamics simulation, and bioactivity validation assessment Z195914464 as a 3CL Mpro inhibitor","authors":"Xiongpiao Wei ,&nbsp;Min Li ,&nbsp;Yuanbiao Tu ,&nbsp;Linxiao Wang","doi":"10.1016/j.bpc.2024.107357","DOIUrl":"10.1016/j.bpc.2024.107357","url":null,"abstract":"<div><div>Discovering novel class anti-SARS-CoV-2 compounds with novel backbones is essential for preventing and controlling SARS-CoV-2 transmission, which poses a substantial threat to the health and social sustainable development of the global population because of its high pathogenicity and high transmissibility. Although the potential mutation of SARS-CoV-2 might diminish the therapeutic efficacy of drugs, 3CL Mpro is the target highly conservative in contrast with other targets. It is an essential enzyme for coronavirus replication. Based on this, this study utilized the drug discovery strategy of Knime molecular filtering framework, ROC-guided virtual screening, clustering analysis, binding mode analysis, and activity evaluation approaches to identify compound <strong>Z195914464</strong> (IC₅₀: 7.19 μM) is a novel class inhibitor of anti-SARS-CoV-2 against the 3CL Mpro target. In addition, based on molecular dynamics simulations and MMPBSA analyses, discovered that compound <strong>Z195914464</strong> can interact with more key residues and lower bonding energies, which explains why it exhibited more activity than the other three compounds. In summary, this study developed a method for the rapid and accurate discovery of active compounds and can also be applied in the discovery of active compounds in other targets.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"317 ","pages":"Article 107357"},"PeriodicalIF":3.3,"publicationDate":"2024-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142746584","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":"Cholesterol modulates the interaction of sodium salt with negatively charged phospholipid membrane","authors":"Kalyan Kumar Banerjee,&nbsp;Pabitra Maity,&nbsp;Surajit Das,&nbsp;Sanat Karmakar","doi":"10.1016/j.bpc.2024.107354","DOIUrl":"10.1016/j.bpc.2024.107354","url":null,"abstract":"<div><div>We present a systematic study on how alkali metal salts, like NaCl and NaI, affect negatively charged phospholipid vesicles using a range of experimental methods. Our goal was to find out how chain saturation and cholesterol affect the interaction between the ions and the membrane. An isothermal titration calorimetry study on large unilamellar vesicles made from dimyristoyl phosphatidylcholine (DMPC) revealed that Na⁺ shows higher binding affinity to the gel phase at 15 °C compared to the fluid phase at 30 °C. Further, cations also show stronger affinity to the membrane in the fluid composed of saturated lipids than that of unsaturated lipids. The binding affinity of Na + with anionic vesicles prepared from a mixture of DMPC and DMPG was found to decrease significantly with increasing cholesterol as well as salt concentrations, as revealed by the zeta potential study. Besides the binding constant, the Gouy Chapman theory based on the electrostatic double layer shows that cholesterol reduces the surface charge density without altering the significant area per molecule. Further, the effect of counterions was investigated using fluorescence spectroscopy of an environment-sensitive lipophilic dye, nile red. Although cholesterol alters the emission properties of nile red significantly, there is no significant change in the presence of ions. This result suggests that anions do not bind significantly to anionic vesicles. The main striking feature of the ion-membrane interaction in the presence of cholesterol is that membranes with saturated lipids exhibit a completely opposite trend from membranes with unsaturated lipids.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"317 ","pages":"Article 107354"},"PeriodicalIF":3.3,"publicationDate":"2024-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142695132","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":"Multispectral analysis and molecular docking of a zinc (II) complex interaction with bovine serum albumin and studies on antibacterial properties, and catecholase mimicry of the complex","authors":"Mohd Tameem ,&nbsp;Mohd Amir ,&nbsp;Mohd Muslim ,&nbsp;Ruby Ahmed ,&nbsp;Mo Ahamad Khan ,&nbsp;Musheer Ahmad ,&nbsp;Farman Ali ,&nbsp;Saleem Javed","doi":"10.1016/j.bpc.2024.107355","DOIUrl":"10.1016/j.bpc.2024.107355","url":null,"abstract":"<div><div>This paper presents the synthesis process of a ligand known as 2-(naphthalene-1-yl)-1H-phenanthro[9,10-d]imidazole (NIP) and its metal complex with zinc (II), denoted as FA-128. The structural validation of FA-128 is accomplished through single-crystal X-ray diffraction (XRD). To explore the biological implications, FA-128's interaction with BSA is investigated. This exploration involves fluorescence and UV–vis absorption spectrometry techniques. The outcomes reveal the formation of robust complexes, as FA-128 significantly quenches the inherent fluorescence of BSA. Various aspects are examined, including binding constants, the count of binding sites, thermodynamic parameters, and energy transfer mechanisms. Evident alterations in BSA conformation are detected using synchronous fluorescence and circular dichroism (CD) spectrum techniques. The study proceeds to molecular docking, elucidating binding sites in the FA-128-BSA interaction. Biochemical reactions between metal complexes and proteins often trigger diverse conformational changes in protein structures. This understanding provides crucial insights into the impacts, mechanisms, and systemic transportation of numerous drugs within the body. FA-128 demonstrated superior antibacterial activity against <em>Staphylococcus aureus</em> (ZOI: 10.50 ± 0.50 mm, MIC: 100 μg/mL) and <em>Klebsiella pneumoniae</em> (ZOI: 13.0 ± 0.25 mm, MIC: 50 μg/mL). In addition, FA-128 has been evaluated as a catalytic system in the oxidation of 3,5-di-tert-butylcatechol (3,5DTBC) in a methanol solvent. FA-128 displays good catecholase-like activity with a significant turnover number (k_cat) of 7.56 × 10² h⁻¹, a Michaelis-Menten constant (K_M) of 8.14 × 10⁻⁴ M, and a maximum reaction rate (V_max) of 2.45 × 10⁻⁵ M s⁻¹ under aerobic conditions.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"317 ","pages":"Article 107355"},"PeriodicalIF":3.3,"publicationDate":"2024-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142695145","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":"Analysis of solid-state NMR data facilitated by MagRO_NMRViewJ with Graph_Robot: Application for membrane protein and amyloid.","authors":"Naohiro Kobayashi ,&nbsp;Yoshitaka Ishii","doi":"10.1016/j.bpc.2024.107356","DOIUrl":"10.1016/j.bpc.2024.107356","url":null,"abstract":"<div><div>Solid-state NMR (ssNMR) methods have continued to be developed in recent years for the efficient assignment of signals and 3D structure modeling of biomacromolecules. Consequently, we are approaching an era in which vigorous applications of these methods are more widespread in research, including functional elucidation of biomacromolecules and drug discovery. However, multidimensional ssNMR methods are not as advanced as solution NMR methods, especially for automated data analysis. This article describes how a newly developed Graph_Robot module, implemented in MagRO-NMRViewJ, evolved from integrated tools for NMR data analysis named Kujira (developed by Kobayashi et al. [<span><span>1</span></span>]). These packaged tools systematically utilize flexible, sophisticated, yet simple libraries that facilitate only for solution-NMR data analysis, offering an intuitive interface accessible even to novice users. In this study, semi-automated assignments of backbone and side chain signals of ssNMR datasets for uniformly ¹³C/¹⁵N labeled aquaporin Z and 42-residue amyloid-β fibril were examined as examples to demonstrate how Graph_Robot can expedite the visual inspection and handling of multidimensional ssNMR spectral data. In addition, the functionality of the Graph_Robot system enables a computer to interpret the behavior of magnetization transfer based on a finite automaton model.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"318 ","pages":"Article 107356"},"PeriodicalIF":3.3,"publicationDate":"2024-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142784056","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":"Functional characterization of Staphylococcus aureus lipase 2 (SAL2) as a collagen adhesin","authors":"T. Priyadharshini ,&nbsp;Sreejanani Sankar ,&nbsp;Karthe Ponnuraj","doi":"10.1016/j.bpc.2024.107352","DOIUrl":"10.1016/j.bpc.2024.107352","url":null,"abstract":"<div><div>Extracellular lipases of many pathogens have been characterized as human virulence factors. <em>Staphylococcus aureus</em> produces a variety of enzymes that aid in the pathogenesis of the bacterium to invade and destroy host tissues, resulting in a wide range of clinical illnesses. The lipase is one such enzyme, and the lipases produced by <em>S. aureus</em> (SAL1, SAL2 and SAL3) have been associated with the virulence of the bacterium. In the present study, we cloned, expressed and purified the mature lipase domain of SAL2 (rSAL2₂₉₆_–₆₉₀) and characterized its interaction with human collagen type IV using biolayer interferometry (BLI), molecular docking and simulation studies. Collagen binds to rSAL2₂₉₆_–₆₉₀ with an affinity of 3.261 μM. The enzymatic activity of rSAL2₂₉₆_–₆₉₀ was analyzed in the presence of collagen and orlistat, a potent lipase inhibitor. The activity of rSAL2₂₉₆_–₆₉₀ in the presence of collagen or orlistat was nearly 90 fold lower than that of the native rSAL2₂₉₆_–₆₉₀. The optimal pH and temperature for rSAL2₂₉₆_–₆₉₀ activity were found at 7 and 25 °C respectively. rSAL2₂₉₆_–₆₉₀ found to be stable at pH 7 and exhibits thermostability in the temperature range 15–25 °C. With CaCl₂ and ZnCl₂, an increase in activity of rSAL2₂₉₆_–₆₉₀ was observed whereas NiSO₄, CuSO₄, MnCl₂, CoCl2 and MgCl₂ reduced the activity. No substrate specificity was found with rSAL2₂₉₆_–₆₉₀, as it cleaves different substrate lengths (C2, C6, C12 and C16) and triglyceride triolein. Interaction of rSAL2₂₉₆_–₆₉₀ with metal-incubated collagen revealed that the binding affinity of collagen in the presence of NiSO₄, CuSO₄ and CoCl₂ significantly reduced. Enzymatic and collagen binding studies provided insights into the putative collagen binding site on SAL2₂₉₆_–₆₉₀, which is near the active site region of the molecule. This study thus revealed that rSAL2₂₉₆_–₆₉₀ as a bi-functional molecule, acts not only as a lipase but also as a collagen adhesin.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"317 ","pages":"Article 107352"},"PeriodicalIF":3.3,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142685942","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 conformational behavior and membrane-destabilizing capability of the antimicrobial peptide ecPis-4s","authors":"K.R. de Souza ,&nbsp;L.O. Nunes ,&nbsp;E.S. Salnikov ,&nbsp;H.M. Mundim ,&nbsp;V.H.O. Munhoz ,&nbsp;L.M. Lião ,&nbsp;C. Aisenbrey ,&nbsp;J.M. Resende ,&nbsp;B. Bechinger ,&nbsp;R.M. Verly","doi":"10.1016/j.bpc.2024.107353","DOIUrl":"10.1016/j.bpc.2024.107353","url":null,"abstract":"<div><div>Here we present studies of the structure and membrane interactions of ecPis-4 s, a new antimicrobial peptide from the piscidin family, which shows a wide-range of potential biotechnological applications. In order to understand the mode of action ecPis-4 s, the peptide was chemically synthesized and structural investigations in the presence of anionic POPC:POPG (3:1, mol:mol) membrane and SDS micelles were performed. CD spectroscopy demonstrated that ecPis-4 s has a high content of helical structure in both membrane mimetic media, which is in line with solution NMR spectroscopy that revealed an amphipathic helical conformation throughout the entire peptide chain. Solid-state NMR experiments of ecPis-4 s selectively labeled with ¹⁵N/²H and reconstituted into uniaxially oriented POPC:POPG membranes revealed an ideal partition of hydrophilic and hydrophobic residues within the bilayer interface. The peptide aligns in parallel to the membrane surface, a topology stabilized by aromatic side-chain interactions of the Phe-1, Phe-2 and Trp-9 with the phospholipids. ²H NMR experiments using deuterated lipids revealed that anionic lipid accumulates in the vicinity of the cationic peptide upon peptide-membrane binding.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"317 ","pages":"Article 107353"},"PeriodicalIF":3.3,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142695136","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":"Urineprint of high-altitude: Insights from analyses of urinary biomarkers and bio-physical-chemical features of extracellular vesicles","authors":"Serena Pilato ,&nbsp;Simona Mrakic-Sposta ,&nbsp;Vittore Verratti ,&nbsp;Carmen Santangelo ,&nbsp;Stefano di Giacomo ,&nbsp;Samanta Moffa ,&nbsp;Antonella Fontana ,&nbsp;Tiziana Pietrangelo ,&nbsp;Federica Ciampini ,&nbsp;Sofia Bonan ,&nbsp;Pamela Pignatelli ,&nbsp;Carmine Noce ,&nbsp;Pietro di Profio ,&nbsp;Michele Ciulla ,&nbsp;Danilo Bondi ,&nbsp;Fabrizio Cristiano","doi":"10.1016/j.bpc.2024.107351","DOIUrl":"10.1016/j.bpc.2024.107351","url":null,"abstract":"<div><div>Humans exposed to altitude hypoxia experience dysfunctions of the urinary system. As a non-invasive, easily manageable and informative biological sample, urine represents a relevant matrix for detecting clinical impairments of urinary system, as well as alterations of other systems and extracellular vesicles (EVs) biology during high-altitude expeditions. Nevertheless, gaps exist in the comprehensive assessment of dysfunction, molecular burden and EVs biology due to high-altitude acute exposure. This study aimed to find a biophysical and biochemical signature of urinary EVs for hypoxia-induced changes in urinary function, putatively accompanied by an oxinflammatory burden. Urine samples of 15 participants were sampled at low and high-altitude during an Alpine project (7 women and 8 men, aged 24-to-63 years and with BMI 17.93-to-30.76 kg/m²) and analysed for: creatinin and albumin, lipid peroxidation, IL6, NO derivatives; atomic force microscopy and Raman spectroscopy were carried out after urinary EVs were isolated through sucrose-gradient ultracentrifugation. Albumin-to-creatinin ratio increased at high altitude, as did IL6 and 8-isoprostane. AFM showed a globular and flattened shape of EVs, although several samples were characterized by a lot of contaminants and EVs lost their prototypal spherical shape; EVs comprehensively maintained their morphology at high altitude. Raman spectroscopy revealed some typical phospholipidic-like pattern, often masked by contaminants of spectra that most often refer to high-altitude samples. Collectively, short-term exposure to altitude hypoxia increased renal concentrating ability, produced non-pathological impairment or renal function, and triggered an oxyinflammatory burden with heterogeneous response of NO system. The combination of AFM and Raman spectroscopy revealed that EVs collected at high altitude more likely are fused together and incorporated into a sediment matrix, and contain contaminants peaks that make the purification process less efficient. The combination of analytical procedures as in the present study offers novel possibilities to detect the biological and clinical effects of high altitude on renal system.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"316 ","pages":"Article 107351"},"PeriodicalIF":3.3,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142647000","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}