Journal of Biomolecular Structure & Dynamics最新文献

{"title":"Exploring tryptamine derivatives as potential agents for diabetes and cancer treatment: <i>in-vitro</i> kinetics, molecular docking, and cell toxicity based investigations.","authors":"Majid Khan, Atta Ullah, Sobia Ahsan Halim, Muhammad Waqas, Abida Mushtaque, Shah Mulk, Fearoz Khan, Li Gao, Asaad Khalid, Arsalan Nizamani, Hamdy Kashtoh, Ajmal Khan, Ahmed Al-Harrasi","doi":"10.1080/07391102.2025.2513013","DOIUrl":"https://doi.org/10.1080/07391102.2025.2513013","url":null,"abstract":"<p><p>Abnormal glucose levels in diabetes mellitus cause chronic complications like neuropathy, nephropathy, retinopathy, cataract, and cardiovascular issues. Aldose reductase (AR), an enzyme in the polyol pathway, is crucial for developing treatments for diabetic complications. To this end, a series of twenty inhibitors based on tryptamine scaffolds were synthesized and assessed for their efficacy in inhibiting AR activity. The compounds showed strong to moderate inhibition of AR with IC₅₀ values ranging from 0.07 µM to 8.11 µM. Among these analogs, <b>3</b> showed the highest IC₅₀ value (0.07 ± 0.9 µM), and <b>1</b> showed the weakest inhibition of AR (IC₅₀ = 8.11 ± 0.7 µM). Furthermore, the cytotoxic potential of these analogs was tested in human fibroblast cells (BJ cell line), where all the compounds showed no toxic effect. Having the advantage of the non-toxic factor of the compounds, these molecules were further tested for anti-cancerous activity in glioblastoma multiforme (GBM) cell line U87. Compounds <b>1-5</b>, <b>14</b>, <b>17</b>, and <b>20</b> showed significant inhibitory effects on the growth of U87 cells in various concentrations, whereas compounds <b>6</b>, <b>11</b> and <b>18</b> showed moderate inhibition. <i>In-vitro</i> mechanistic studies show that compounds have competitive mode of inhibition for AR. Furthermore, molecular docking studies reveal that these compounds fit appropriately into the active site of AR. Finally, our study explores the stability and binding affinities of selected tryptamine-based inhibitors of AR using molecular dynamics simulations, identifying compounds <b>2</b> and <b>3</b> as promising candidates for therapeutic development.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-24"},"PeriodicalIF":2.7,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144284514","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":"Synthesis, structure, DNA docking, pharmacokinetics/ADMET, Hirshfeld surface analysis, and antimicrobial studies on biphenyl appended pyrrolidine complexes.","authors":"Koyal Pattanaik, Popuri Sureshbabu, Elanseralathan Sujitha, Suman Bhattacharya, Shahulhameed Sabiah","doi":"10.1080/07391102.2025.2508921","DOIUrl":"https://doi.org/10.1080/07391102.2025.2508921","url":null,"abstract":"<p><p>Biphenyl anchored pyrrolidine complexes [MLCl₂], [where M = Co (<b>1</b>), Ni (<b>2</b>), Cu (<b>3</b>) and Zn (<b>4</b>); <b><i>L</i> </b>=<b> </b>6-(2-(pyrrolidin-1-yl)ethyl)-6,7-dihydro-5H-dibenzo[c,e]azepine] were synthesized and characterized by elemental analysis, UV-Vis, FT-IR, ESI-MS, and NMR (in case of <b>4</b>). Single crystal XRD revealed that all the complexes adopt distorted tetrahedral geometry. DFT calculations with their relative energies were compared with XRD structure. Absorption, oscillator strength, excitation energy, molecular orbital contributions were obtained from TDDFT calculation. The computed UV-Vis absorption data is comparable with experimental UV-Vis data. Molecular docking studies verified that all complexes strongly bind with DNA (PDB ID: 1BNA) through major groove interactions. The ligand and the complexes exhibit an elevated permeability of the blood-brain barrier and GI absorption, according to the SwissADME prediction criteria. The values of skin permeability (logKp) for the ligand and complexes <b>1-4</b> were determined to be -5.61, -5.27, -5.27, -5.30, and -5.31 cms^-1, respectively. All the complexes and the ligand were projected to function as a biological barrier, a transporter, and a substrate of P-glycoprotein (P-gp), which is responsible for the ADME of medications. Using Hirshfeld surface investigation, the intermolecular interactions within the crystal network were identified to support the prominent contribution from H∙∙∙∙∙H interactions, followed by Cl∙∙∙∙∙H and C∙∙∙∙∙H interactions, respectively. In the preliminary investigations, all the complexes displayed significant antibacterial properties against both Gram-positive and Gram-negative bacterial strains such as Staphylococcus aureus and Escherichia coli, respectively; those were obtained from human clinical isolates. Notably, the copper(II) complex, <b>3</b> showed better antibacterial activity in comparison to other complexes.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-20"},"PeriodicalIF":2.7,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144284516","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":"Exploring the coupling of dynamic residues in TEM-1 β-lactamase and their role in activity.","authors":"Fatma Gizem Avci, Didem Vardar Ulu, Basak Atas Erden, Fatma Ece Altinisik Kaya, S Banu Ozkan, Berna Sariyar Akbulut","doi":"10.1080/07391102.2025.2516144","DOIUrl":"https://doi.org/10.1080/07391102.2025.2516144","url":null,"abstract":"<p><p>The increase in the incidence of β-lactamase enzymes resistant to inhibitors has elevated the search for novel therapeutic strategies, particularly those that target amino acid residues other than the active site. In this respect, correlated amino acids that tend to evolve and have direct or indirect communication with the active site are considered potential candidates. Thus, this study identified residues that are dynamically coupled to the active site of TEM-1 β-lactamase by using the dynamic coupling index. These residues were found to cluster in three distinct structural regions: in a loop close to one face of the active site (D214, K215, and V216), at the binding interface with β-lactamase inhibitory protein close to a second face of the active site (E104, Y105, S106, E110, T114), and on a β-strand at the N-terminus, distant from the active site (R43, V44). Representative residues, K215, E104, E110, T114, and R43, were selected for mutational analysis to assess their roles in enzyme activity. Notably, the mutation of R43 to alanine led to a significant reduction in activity, with up to 70%. To assess the role of the positive charge at R43, the R43K and R43E point mutants were generated, both of which exhibited complete loss of enzymatic activity. Circular dichroism analyses, thermal melting experiments, and the low expression levels pointed out a loss of stability for R43 mutants. These findings highlight R43 as a promising new target for the development of alternative β-lactamase inhibitors.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-11"},"PeriodicalIF":2.7,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144284513","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":"Integrative computational and experimental approaches for identifying potent antimalarials by targeting falcipain-2 of <i>Plasmodium falciparum</i>.","authors":"Haider Thaer Abdulhameed Almuqdadi, Mohd Shakir, Rumaisha Shoaib, Jihad Alrehaili, Razique Anwer, Shailja Singh, Mohammad Abid","doi":"10.1080/07391102.2025.2516143","DOIUrl":"https://doi.org/10.1080/07391102.2025.2516143","url":null,"abstract":"<p><p>Malaria remains a critical global health issue, particularly in tropical and subtropical regions. Understanding its biology and epidemiology is vital for developing effective prevention and control strategies. Falcipain-2 (FP-2), a cysteine protease in <i>Plasmodium falciparum</i>, the deadliest malaria parasite, is essential for parasite survival in red blood cells, making it an attractive drug target. Inhibiting FP-2 disrupts key metabolic processes, leading to parasite death, offering a promising antimalarial drug development avenue. This study utilized computational approaches to design novel antimalarials. We prepared large fragment libraries, Enamine (∼220,174 fragments) and ChemDiv (∼18,713 fragments), for virtual screening against FP-2 (PDB ID: 6JW9). Fragments with binding free energies ≤ -4.0 kcal/mol were selected and evolved into drug-like ligands. SP and XP docking-based screenings prioritized these ligands, refined further using MM-GBSA calculations. Promising ligands underwent 100 ns molecular dynamics simulations to assess conformational changes and complex stability. This study identified two viable inhibitors, <b>T4</b> and <b>A3</b>, with high affinity, stability, and selectivity towards FP-2 compared to E64.Following computational studies, compound <b>A3</b> and its ten analogues (<b>KA-series</b>) were synthesized and characterized by using multi-spectroscopic techniques with high purity confirmed by LC-MS. Biological testing against <i>P. falciparum</i> 3D7 strain revealed <b>KA-5</b> as the most potent compound with an IC₅₀ value of <b>3.0 μM</b>. Future work will involve synthesizing additional analogue series for an extensive structure-activity relationship (SAR) study. Further experimental validation is essential to develop these compounds as effective therapeutic agents for malaria treatment.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-20"},"PeriodicalIF":2.7,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144284515","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":"'Unlocking the potential of cefuroxime axetil metal complexes: a multifaceted approach to discovering <i>β</i>-glucosidase inhibitors through MD simulations, POM analyses, and pharmacophore site identification'.","authors":"Mehwish Pari, Rizwana Sarwar, Syed Majid Bukhari, Sara Khan, Nadia Riaz, Aneela Khushal, Faisal A Almalki, Taibi Ben Hadda, Umar Farooq, Asaad Khalid, Hamdy Kashtoh, Ajmal Khan, Tanveer A Wani, Ahmed Al-Harrasi","doi":"10.1080/07391102.2025.2513572","DOIUrl":"https://doi.org/10.1080/07391102.2025.2513572","url":null,"abstract":"<p><p>Due to the poor bioavailability of Cefuroxime axetil, the current study explored the synthesis of complexes of a Cefuroxime axetil with metal ions thereby increasing their biological activities. This structural modification on the one hand solves the solubility problem and on the other hand may tend to improve the pharmacology, toxicology, and other physio-chemical properties of the drug. Cefuroxime-loaded metal complexes <b>(1-6)</b> of CrBr₃.6H₂O, CoCl₂.6H₂O, CuCl₂, MnCl₂.H₂O, NiCl₂.H₂O, and ZnCl₂ were synthesized in equimolar ratios where the drug acts as a bis-bidentate ligand. These complexes were characterized by using UV-<i>Vis</i>, FT-IR, and TGA. The synthesized metal complexes were subjected to enzyme inhibition assay targeting <i>β</i>-glucosidase. The Cefuroxime-copper (II) complex was found to be 5 times more active as compared to the free ligand, and almost 1.2 times more active compared to the standard drug. The binding energy of a ligand with a metal ion provides insight into the complicated molecular processes involved in the binding of protein-metal complexes through in-silico study. The criteria set forth for the confirmation were binding energy ΔG, and root mean square deviation using MoE software. Molecular docking study reveals the binding energy of ligands with metal ions. MD simulations unveiled a robust binding affinity between the inhibitors and the active site of <i>β</i>-glucosidase, inducing notable structural conformational alterations within the protein. Conclusively, These metal complexes have a greater capacity to block <i>β</i>-glucosidase activity than standard drugs, as evidenced by their binding energy and interaction pattern inside the active pocket, making them a better drug candidate.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-15"},"PeriodicalIF":2.7,"publicationDate":"2025-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266251","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":"Investigating resveratrol-lipase interactions through multispectral analysis and molecular docking studies.","authors":"Menghan Wang, Xiaoxia Wang, Jisheng Sun, Zhihua Nie, Wenxiu He, Jianguo Cheng, Jianguo Duan","doi":"10.1080/07391102.2025.2514699","DOIUrl":"https://doi.org/10.1080/07391102.2025.2514699","url":null,"abstract":"<p><p>Resveratrol (RES), a natural polyphenol with diverse pharmacological properties, has shown potential in modulating lipid metabolism through interactions with lipase (LPS). This study employed multispectral techniques and molecular docking to characterize the RES-LPS interaction mechanism quantitatively. Fluorescence quenching analysis revealed static quenching with a binding constant (<i>K_A</i>) of 7.499 × 10⁵ L·mol^-1 at 298 K, supported by thermodynamic parameters (Δ<i>G</i> = -40.43 kJ·mol^-1, Δ<i>H</i> = -44.26 kJ·mol^-1, Δ<i>S</i> = -135.5 J·mol^-1·K^-1), indicating spontaneous, exothermic binding driven by hydrogen bonds and van der Waals forces. UV-vis spectroscopy demonstrated a 2 nm redshift in LPS's absorption peak, confirming complex formation. Circular dichroism revealed RES-induced secondary structural changes in LPS, with α-helix content decreasing from 17.2% to 17.0% and random coils increasing from 41.6% to 42.9%. Molecular docking identified key binding residues (ARG256, ASP79, TRP252) and a binding free energy of -3.86 kcal·mol^-1, validating the experimental findings. These results provide a mechanistic basis for RES's role in lipid metabolism regulation and its potential therapeutic applications.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-13"},"PeriodicalIF":2.7,"publicationDate":"2025-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266248","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":"Identification of phytochemicals in <i>Nyctanthes arbor-tristis</i> leaf: interpreting antidiabetic and antibacterial effect through <i>in vitro</i> and <i>in silico</i> analysis.","authors":"Chandramohan Govindasamy, Shahitha Sikkandar, Khalid S Al-Numair, Mohammed A Alsaif, Chitra Loganathan","doi":"10.1080/07391102.2025.2507817","DOIUrl":"https://doi.org/10.1080/07391102.2025.2507817","url":null,"abstract":"<p><p><i>Nyctanthes arbor-tristis</i> is a traditional medicinal plant in India; however, it is least explored for biological activities. In the present study, antioxidant, mammalian alpha-glucosidase (AG) inhibition, and antibacterial activity of <i>N. arbor-tristis</i> leaf (NL) were determined by <i>in vitro</i> and <i>in silico</i> analysis. Methanolic extract of NL (ME-NL) was prepared. The phytochemical constituents present in ME-NL were tentatively identified using LC-ESI/MS/MS analysis. The inhibition of mammalian AG activities (maltase, sucrase, isomaltase and glucoamylase) and the antibacterial activity of ME-NL were analyzed. Virtual screening of compounds identified in ME-NL for the interaction with human AG (hAG), <i>Escherichia coli</i> dihydropteroate synthase (EDHPS) and <i>Staphylococcus aureus</i> DHPS (SDHPS) was carried out. The best scored four compounds with respective proteins were subjected to molecular dynamics (MD) simulation, post-MD analysis (RMSF, RMSD, 2D-RMSD, PCA, DCCM and FEL) and MM/GBSA analysis. ME-NL was found to be rich in various phenolics and flavonoid compounds. ME-NL showed radical scavenging and ferric reducing antioxidant power activities. ME-NL inhibited all the mammalian AG activities in microgram/ml concentration through a mixed-type of inhibition. ME-NL inhibited both gram-positive and gram-negative bacteria. From the <i>in silico</i> analysis, it was found that among the compounds studied, 3-(4-Hydroxy-3-methoxyphenyl)-1,2-propanediol 2-O-(galloyl-glucoside) (HMPGG) showed stable interactions with hAG and SDHPS; Prupaside (PRU) with hAG; desrhamnosylmartynoside (DRM) with EDHPS; calceolarioside A (CAL) with SDHPS and luteolin 7-rhamnosyl (1->6) galactoside (LRG) with both EDHPS and SDHPS. Altogether, <i>in vitro</i> and <i>in silico</i> analysis revealed the antidiabetic and antibacterial effects of ME-NL, which warrant further <i>in vivo</i> studies.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-19"},"PeriodicalIF":2.7,"publicationDate":"2025-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266247","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":"Unleashing the potential of Arabian camel milk proteins: virtual screening confirms putative peptidome as highly effective anti-tubercular peptides.","authors":"Adeela Kanawati, Fernando Zanchi, Haitham Ahmed Al-Madhagi","doi":"10.1080/07391102.2025.2516139","DOIUrl":"https://doi.org/10.1080/07391102.2025.2516139","url":null,"abstract":"<p><p>Despite the testing of various small molecules and new drug entities, tuberculosis still represents a major health burden given the fact that it kills > 40.000 cases every single day. In the recent years, antimicrobial peptides (AMP) were proved their extraordinary activity against different bacterial species. In the present study, we examined the peptidome of Arabian camel milk proteins as AMP through computer-aided drug development approaches. Five proteins from Arabian camel milk sequences were downloaded from UniProt database followed by <i>in silico</i> digestion using AHPP server. The generated peptides were assessed for their anti-TB activity, biochemical properties, allergenicity, toxicity and membrane penetrability. Peptides passed fulfilled these criteria were then subjected to molecular docking <i>via</i> HPEPDOCK 2 and CABS-dock tools. Afterward, molecular dynamics (MD) were performed for best docked complex to assess the stability. Of the generated peptidome, only four peptides proved anti-TB activity, non-allergen, non-toxic and classified as cell-penetrating peptides. The five peptides were the best in terms of docking to thymidylate kinase and found to be stable after 120 ns of MD simulations as reflected by the low RMSD and RMSF change (< 0.5 nm). The putative peptidome of Arabian camel milk proteins is a potential AMP against <i>M. tuberculosis</i> but needs <i>in vitro</i> experimentation.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-11"},"PeriodicalIF":2.7,"publicationDate":"2025-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266250","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":"Peptide-mediated stabilization of <i>Trichoderma reesei</i> Cel7A for enhanced thermal stability in bioethanol production.","authors":"Bader Huwaimel, Kareem M Younes, Amr S Abouzied","doi":"10.1080/07391102.2025.2514705","DOIUrl":"https://doi.org/10.1080/07391102.2025.2514705","url":null,"abstract":"<p><p>Improving the thermal stability of <i>Trichoderma reesei</i> Cel7A, a key cellulase for bioethanol production, is crucial for reducing costs and enhancing efficiency under industrial conditions. While Cel7A functions optimally at moderate temperatures (40-50 °C), its activity diminishes at higher ranges (50-80 °C). This study integrates Molecular Dynamics (MD) simulations, Machine Learning (ML) predictions, and Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) free energy calculations to develop a peptide-mediated stabilization strategy. Analysis of root mean square fluctuations (RMSF) at 350K identified thermally sensitive, flexible regions. Surface-accessible area calculations pinpointed a stretch of residues (TYPTNETSTPG) for targeted mutations, generating 69,984 peptides. Screening with ML-based DeepPurpose, clustering, and similarity analyses yielded 15 candidates. Docking and ΔSASA calculations highlighted three promising peptides (Peptide-7, Peptide-10, and Peptide-15) with binding free energies of -27.33, -11.07, and -7.36 kcal/mol, respectively. Density Functional Theory (DFT), MD simulations, and QM/MM analyses revealed Peptide-15 as the most stable candidate, displaying strong polar interactions, high dipole moment (447.49 Debye), and consistent energetic stabilization. Its integration with Cel7A achieved thermal stability, suggesting that peptide-based stabilization is a viable method to enhance enzyme performance in bioethanol systems under heat stress.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-25"},"PeriodicalIF":2.7,"publicationDate":"2025-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144266249","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 fatty acid and ketone arise albumin structure recovery caused by furosemide.","authors":"Yafang Wei, Neng Zhou","doi":"10.1080/07391102.2025.2513570","DOIUrl":"https://doi.org/10.1080/07391102.2025.2513570","url":null,"abstract":"<p><p>Applied various spectroscopic techniques, such as fluorescence spectroscopy and circular dichroism, etc., the interaction between furosemide (FU) and bovine serum albumin (BSA), as well as the effects of long-chain fatty acid and ketone on the conformational changes of BSA induced by furosemide were studied. The results showed that furosemide strongly quenched the endogenous fluorescence of BSA. Fatty acid sites 7, 6, and/or 1 were the high affinity sites of FU, while its low affinity sites were not in the vicinity of the seven binding sites of oleic acid. When FU binds to high affinity sites, it can cause decrease of the percentage of α-helices, while binding to its low affinity sites leads to tertiary structural change. The binding of FU induces a significant red shift in the maximum fluorescence wavelength, indicating that it triggers a change in the tertiary structure. Long chain fatty acids and ketones have a restorative effect on the tertiary structural changes of BSA induced by FU in different mechanisms and this recovery does not originate from the alteration of the percentage of α-helices.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-14"},"PeriodicalIF":2.7,"publicationDate":"2025-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144248038","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}