Journal of Biomolecular Structure & Dynamics最新文献

{"title":"Theoretical conformational analysis of cross-linking bonds in fungal hydrophobin from <i>Aspergillus fumigatus</i>.","authors":"Fabiola E Medina, Juana Coloma, Claudia Oviedo","doi":"10.1080/07391102.2025.2496289","DOIUrl":"https://doi.org/10.1080/07391102.2025.2496289","url":null,"abstract":"<p><p><i>Aspergillus fumigatus</i> is a common saprophytic filamentous fungus that plays a crucial role in nutrient cycling but can become an opportunistic pathogen, posing a significant threat to immunocompromised individuals by causing invasive aspergillosis. A key feature of <i>A. fumigatus</i> is the presence of hydrophobins-small amphipathic proteins that form a protective rodlet layer on conidial surfaces, facilitating biofilm formation and immune evasion. This rodlet structure, stabilized by cross-linking disulfide bonds, provides resistance to desiccation, oxidative stress, and immune defenses, making these cross-links a compelling target for study. In this work, we employ all-atom simulations, incorporating quantum mechanics/molecular mechanics (QM/MM) calculations, to evaluate the energy and conformational effects of cross-linking disulfide bonds (CL1, CL2, CL3, and CL4) in the rodlet assembly. By integrating QM/MM approaches, we achieve a detailed representation of the electronic and structural properties of these bonds within the complex rodlet layer, gaining deeper insights into their essential role in maintaining the stability and integrity of the <i>RodA</i> hydrophobin protein from <i>A. fumigatus</i> conidial surface. We identify a group of ten residues that influence directly in the cross-linking, with Gln23 and Lys17 emerging as key candidates for experimental mutation to control rodlet assembly. Our findings shed light on the molecular mechanisms underlying rodlet formation and highlight potential targets for disrupting this protective layer, offering promising avenues for antifungal strategies.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-10"},"PeriodicalIF":2.7,"publicationDate":"2025-04-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144019812","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":"Phytoconstituents from <i>Artemisia annua</i> medicinal plant as potent inhibitors targeting Salmonella SpvB: a molecular docking and dynamic study.","authors":"Fawaz M Almufarriji, Bader S Alotaibi, Ahlam Saleh Alamri, Samia S Alkhalil, Maher S Alwethaynani","doi":"10.1080/07391102.2025.2492237","DOIUrl":"https://doi.org/10.1080/07391102.2025.2492237","url":null,"abstract":"<p><p>Salmonella, a genus with a global presence, is a leading cause of diarrheal diseases in both humans and animals. With over 2,400 distinct serotypes, most exhibiting minimal host specificity, Salmonella infection remains a significant public health issue. It poses a substantial economic burden on both developed and developing nations due to the costs associated with disease surveillance, prevention, and treatment. To address this global challenge, it is essential to explore cost-effective therapeutic interventions derived from medicinal plants. In this study, we targeted the Salmonella SpvB ATR domain for molecular docking of phytochemical compounds. A library of 392 phytochemical compounds from the Artemisia annua (Sweet wormwood) medicinal plant was utilized. In the initial screening, the top 20 phytochemical compounds were selected based on their high binding affinity toward SpvB. These 20 compounds underwent interaction analysis, revealing that two compounds, IMPHY004808 and IMPHY015047, formed crucial interactions. The IMPHY004808 compound bound at binding site residues ARG414, ARG471, LEU473, and GLU538, with residue SER501 present at the active site. Similarly, the IMPHY015047 compound formed bonds at binding site residues ARG471, ARG414, GLY472, and GLU538, while residue SER501 was present at the active site of SpvB. The trajectory analysis of 500 ns MD simulation, including deviation, fluctuation, compactness, surface area calculation, secondary structure element alterations, and hydrogen bond analysis, showed that the complexes were stable during the simulation time. Moreover, PCA with minimal vibration, FEL analysis and MMPBSA analysis strongly recommend that the complexes were stable and further validation with experimentation is needed.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-14"},"PeriodicalIF":2.7,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143973041","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":"Bioactive fungal compounds as potential anti-HIV agents against HIV-1 protease: a multi-faceted molecular modelling approach for drug discovery.","authors":"Madhusmita Panda, Priyanka Purohit, Debashis Barik, Jarmani Dansana, Biswa Ranjan Meher","doi":"10.1080/07391102.2024.2333986","DOIUrl":"https://doi.org/10.1080/07391102.2024.2333986","url":null,"abstract":"<p><p>HIV-PR is a prominent pharmacological target that is driving the development of various possible HIV inhibitors. Unfortunately, the viral strain population has evolved to be even more resistant to medications; therefore, studying the dynamic structures of both WT and mutant viruses, besides their interactions with inhibitors, may be advantageous. Molecular dynamics analyses and free-energy calculations on the WT and four important resistance mutants (V82F, I84V, I50V, and V82F/I84V) of HIV-PR complexed with fungal compounds were performed to completely examine the mechanism of HIV-PR drug resistance. To determine precise binding free energies, we utilized an MM/GBSA method based on molecular mechanics. In this study, we found that compared to WT and single mutants, the double mutant (V82F/I84V) exhibited less flexibility and less curling of the flap tips. Contradiction with prior studies, our data reveal that the double mutant (V82F/I84V) facilitates binding affinity, suggesting that this variant may be particularly well suited to Ganomycin-I. The energy decomposition study shows that an increase in E_vdw energy by 6.56 kcal/mol is responsible for much of the increased binding observed for the double mutant (V82F/I84V) HIV-PR, which plays a direct role in increasing the binding affinity by approximately -1.62 (Val82' to Phe82') and -1.08 (Ile84' to Val84') kcal/mol, accounts for 41% of the total gain of the binding affinity. In addition to the direct impacts of Phe82' and Val84', the residues Gly27, Ala28, Asp29, Asp30, Ile47, and Ile50 each contribute more than -1 kcal/mol to the enhanced binding affinity of (V82F/I84V) HIV-PR towards the inhibitor.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-23"},"PeriodicalIF":2.7,"publicationDate":"2025-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144036552","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":"Structural dynamics of olfactory receptors: implications for odorant binding and activation mechanisms.","authors":"Imlimaong Aier, Nidhi Dubey, Pritish Kumar Varadwaj","doi":"10.1080/07391102.2025.2492235","DOIUrl":"https://doi.org/10.1080/07391102.2025.2492235","url":null,"abstract":"<p><p>Olfaction, an ancient and intricate process, profoundly shapes human innate responses yet remains relatively understudied compared to other sensory modalities. Olfactory receptors (ORs), members of the G protein-coupled receptor (GPCR) family, play a pivotal role in detecting and discriminating a vast array of odorants. This comprehensive study explores the functional roles of five diverse ORs: OR1A1, OR2W1, OR11A1, OR51E1 and OR51E2, through detailed investigations into the differences between their apo and odorant-bound forms. By examining key residues and mutations, the possible molecular mechanisms that underlie the modulation of binding landscapes and the consequent alterations in OR stability were elucidated. The findings revealed dynamic conformational changes in ORs upon odorant binding, characterized by hinging motions and tilting of transmembrane helices. Using residue interaction network analyses, critical residues involved in mediating interactions between ORs and odorants were uncovered, shedding light on the molecular determinants of olfactory perception. By examining changes in binding pocket volume and per-residue energy decomposition, the dynamic nature of OR activation and the influence of mutations on receptor stability and functionality was observed.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-12"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143984876","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":"Deciphering the <i>in silico</i> molecular mechanism of coumestrol activity for uterine fibroids remedy: a promising estrogenic target drug candidate.","authors":"Christopher Busayo Olowosoke, Aqsa Munir, Salimat Opeyemi Sofela, Olachi Lilian Osuagwu, Chioma Joy Eze, Odunayo Taiwo, Valerie Onyia Babatope, Meriem Khedraoui, Oluwafemi Adeleke Ojo, Samir Chtita, Tope Abraham Ibisanmi","doi":"10.1080/07391102.2025.2487191","DOIUrl":"https://doi.org/10.1080/07391102.2025.2487191","url":null,"abstract":"<p><p>Uterine fibroids (UF) are reproductive conditions that occur as tumours in the womb. It is a gynecological outgrowth of diverse sizes often allied with infertility risks that might require surgery to reduce the complication in the worst-case scenario in women. Recent studies have uncovered that estrogen can induce and facilitate other target pathways' action on target cells for UF's pathogenesis, among the targets probed for pharmaceutical intervention. This study screens the interaction effects of 32 phytochemicals from indigenous and adopted potent Chinese plants and herbs; Chamomile, Pomegranate, Red clover, Cinnamomum, and Date palm, against estrogen receptor alpha (ESRα) to serve for anti-UF drug candidates using <i>in silico</i> tools through the molecular mechanisms. The interaction identifies coumestrol as the best-docked candidate (-9.6 kcal/mol) with a correlation to the binding free energy (-30.487 kcal/mol) as compared to the standard drug tamoxifen (-9.3 kcal/mol; -46.928 kcal/mol). The downstream post-docking evaluation reveals coumestrol to have excellent pharmacokinetics, drug-likeness, leadlikeness (no violation), less toxic (LD50; 2991 mg/kg), and highly interactive with ESRα. Coumestrol was top-ranked for ESRα (1QKU) target by PharmMapper among 300 human protein targets, with a z-score of 1.19368. The density functional theory (DFT) and dynamic simulation of 200 ns reveal regions of coumestrol structure and its complex that contribute to the chemical reactivity, stability, flexibility, and compactness of druggability. Ultimately, coumestrol emerged as a potential candidate suitable for anti-UF management, therefore future direction for its application should be on the design and synthesis of new structural derivatives for further <i>in silico</i>, <i>in vitro</i>, and <i>in vivo</i> studies.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-26"},"PeriodicalIF":2.7,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144005645","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":"Amalgamation of experimental strategies, computational simulation, and computer-assisted-theoretical analysis to decipher the interaction of newly synthesized plumbagin-indole-3-propionic ester with cholinesterases.","authors":"Chitra Loganathan, Saravanan Kandasamy, Penislusshiyan Sakayanathan, Fuad Ameen, Ancy Iruthayaraj, Palvannan Thayumanavan","doi":"10.1080/07391102.2025.2490058","DOIUrl":"https://doi.org/10.1080/07391102.2025.2490058","url":null,"abstract":"<p><p>Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are important target proteins to treat cognitive dysfunction in neurodegenerative diseases, such as Alzheimer's disease and Parkinson disease. Hence identification of inhibitors against these proteins is ever-growing. To get a foresight on the potential of a molecule that could be forwarded as a drug candidate, the combinations of bioinformatics [including molecular docking and molecular dynamics (MD) simulation], computer-assisted-theoretical analysis and <i>in vitro</i> strategy were employed to gain knowledge on interaction/inhibition of newly synthesized ester of plumbagin (PLU) and indole-3-propionic acid (IPA) called PLU-IPA with/against AChE and BChE. Density functional theory and ADME analysis revealed the non-toxicity and chemical reactivity gained by the molecule due to esterification and drug-likeness of PLU-IPA. PLU-IPA inhibited AChE and BChE in micromolar concentration through non-competitive mode. In molecular docking, PLU-IPA interacted with amino acids present in sub-pockets near the catalytic site, anionic site, and PAS of electric eel AChE (eAChE), human AChE (hAChE), and hBChE. Through computer-assisted-theoretical analysis, the importance of non-covalent interactions for the proper orientation of PLU-IPA within the active site gorge of AChE/BChE was understood. Further MD simulation results also confirmed the stable interaction of PLU-IPA with AChE/BChE.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-16"},"PeriodicalIF":2.7,"publicationDate":"2025-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144002383","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":"Screening of medicinal phytocompounds with structure-based approaches to target key hotspot residues in tyrosyl-DNA phosphodiesterase 1: augmenting sensitivity of cancer cells to topoisomerase I inhibitors.","authors":"Muhammad Suleman, Abbas Khan, Safir Ullah Khan, Mohammed Alissa, Suad A Alghamdi, Amani Alghamdi, Abir Abdullah Alamro, Sergio Crovella","doi":"10.1080/07391102.2025.2490061","DOIUrl":"https://doi.org/10.1080/07391102.2025.2490061","url":null,"abstract":"<p><p>One of cancer's well-known hallmarks is DNA damage, yet it's intriguing that DNA damage has been explored as a therapeutic strategy against cancer. Tyrosyl-DNA phosphodiesterase 1, involved in DNA repair from topoisomerase I inhibitors, a chemotherapy class for cancer treatment. Inhibiting TDP1 can increase unresolved Top1 cleavage complexes in cancer cells, inducing DNA damage and cell death. TDP1's catalytic activity depends on His263 and His493 residues. Using molecular simulation, structure-based drug design, and free energy calculation, we identified potential drugs against TDP1. A multi-step screening of medicinal plant compound databases (North Africa, East Africa, Northeast Africa, and South Africa) identified the top four candidates. Docking scores for top hits 1-4 were -7.76, -7.37, -7.35, and -7.24 kcal/mol. Top hit 3 exhibited the highest potency, forming a strong bonding network with both His263 and His493 residues. All-atoms simulations showed consistent dynamics for top hits 1-4, indicating stability and potential for efficient interaction with interface residues. Minimal fluctuations in residue flexibility suggest these compounds can stabilize internal flexibility upon binding. The binding free energies of -35.11, -36.70, -31.38, and -23.85 kcal/mol were calculated for the top hit 1-4 complexes. Furthermore, the chosen compounds demonstrate outstanding ADMET characteristics, such as excellent water solubility, effective gastrointestinal absorption, and the absence of hepatotoxicity. Cytotoxicity analysis revealed top hit 2 higher probability of activity against 24 cancer cell lines. Our findings suggest that these compounds (top hits 1-4) hold promise for innovative drug therapies, suitable for both <i>in vivo</i> and <i>in vitro</i> experiments.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-16"},"PeriodicalIF":2.7,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143993475","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":"Design, synthesis and investigation of new imidazole derivatives with biological activities and antifungal effects.","authors":"Sare Peçe, Derya Osmaniye, Begüm Nurpelin Sağlık Özkan, Serkan Levent, Yusuf Ozkay, Zafer Asım Kaplancıklı","doi":"10.1080/07391102.2025.2490059","DOIUrl":"https://doi.org/10.1080/07391102.2025.2490059","url":null,"abstract":"<p><p>Fungal infections are important types of infection that annually cause the death of many people around the world. Therefore, new antifungal agents that are more effective and less toxic are constantly needed. In this study, new imidazole derivatives were synthesized and their antifungal activities were investigated. Compound <b>5d</b> showed antifungal activity against <i>Candida albicans</i>, <i>Candida parapsilosis</i> and <i>Candida krusei</i> with a minimum inhibitory concentration (MIC₅₀) of 0.98 µg/mL. While compound <b>5e</b> showed antifungal effects against <i>C. albicans</i> and <i>C. parapsilosis</i> with MIC₅₀ of 0.98 µg/mL, it displayed potent antifungal activity against <i>C. krusei</i> with MIC₅₀ of 1.96 µg/mL. Compound <b>5h</b> exhibited antifungal activity against <i>C. albicans</i> and <i>C. parapsilosis</i> with MIC₅₀ of 1.96 and 0.98 µg/mL, respectively. It is known that azole group antifungals inhibit ergosterol biosynthesis by inhibiting the 14α-demethylase enzyme. For this reason, in the present study <i>in silico</i> studies were performed on 14α-demethylase enzyme crystal (PDB ID: 1EA1). Molecular docking and dynamics studies were conducted to examine the binding modes of the active compounds (<b>5d</b>, <b>5e</b> and <b>5h</b>). The results of the <i>in silico</i> studies agreed with the biological activity results.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-15"},"PeriodicalIF":2.7,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143982269","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":"Sesamin regulates breast cancer through reprogramming of lipid metabolism.","authors":"Prajakta Patil, Amol Chaudhary, Vishwambhar Vishnu Bhandare, Vishal S Patil, Faizan A Beerwala, Veeresh Karoshi, Kailas D Sonawane, Aniket Mali, Ruchika Kaul-Ghanekar","doi":"10.1080/07391102.2024.2333991","DOIUrl":"https://doi.org/10.1080/07391102.2024.2333991","url":null,"abstract":"<p><p>Metabolic reprogramming is one of the hallmarks of breast cancer (BC), involving elevated synthesis and uptake of lipids, for catering to increased energy demand of cancer cells and to suppress the host immune system. Besides promoting proliferation and survival of BC cells, lipid metabolism reprogramming (LMR) is associated with stemness and chemoresistance. Recently, lignans have been reported for their therapeutic potential against different cancers, including BC. Here, we explored the potential of lignans to target LMR pathways in BC through computational approach. Initially, 88 lignans having potential anticancer activities, underwent druglikeness and pharmacokinetics analysis, displaying promising pharmacokinetic properties, except for 13 molecules with violations. Molecular docking assessed the interaction of 88 lignans (NPACT) with therapeutic targets of LMR including 3-Hydroxy-3-methyl-glutaryl-coenzyme A reductase (HMGCR), Sterol regulatory element-binding proteins 1 and 2 (SREBP1 and 2), Low-density lipoprotein receptor (LDLR), Acetyl-CoA Acetyltransferase 1 (ACAT1), ATP-binding cassette transporter (ABCA1), Liver X receptor α (LXRα), Apolipoprotein A1 (APOA1), Fatty Acid Synthase (FASN), Peroxisome proliferator-activated receptor gamma (PPARG), Stearoyl-CoA desaturase (SCD1), Acetyl-CoA carboxylase 1 and 2 (ACC1/ACACA, and ACC2/ACACB). In silico screening revealed sesamin (SE) as the best-identified hit that showed stable and consistent binding with all the selected targets of LMR. The stability of these complexes was validated by a 100 ns simulation run, and their binding free energy calculation was determined by MM-PBSA method. Interestingly, SE modulated the mRNA expression of genes involved in LMR in BC cell lines, MCF-7 and MDA-MB-231, thereby suggesting its potential as an inhibitor of LMR.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-21"},"PeriodicalIF":2.7,"publicationDate":"2025-04-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143992701","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":"1,2,3-Triazole naphthaldehyde compounds and their oxime derivatives: <i>in vitro</i> and <i>in silico</i> DNA binding properties.","authors":"Ahmet Acuz, Özge Güngör, Derya Kılıçaslan, Seyit Ali Güngör, Muhammet Köse","doi":"10.1080/07391102.2025.2490060","DOIUrl":"https://doi.org/10.1080/07391102.2025.2490060","url":null,"abstract":"<p><p>In this work, we report the synthesis and DNA binding properties of a series of 1,2,3-triazole naphthaldehyde compounds and their oxime derivatives. The 1,2,3-triazole naphthaldehyde compounds (<b>1a-1f</b>) were prepared by the Cu(I) catalysed click reactions. The 1,2,3-triazole naphthaldehyde compounds (<b>1a-1f</b>) were then reacted with hydroxyl amine to yield 1,2,3-triazole oxime compounds (<b>2a-2f</b>). The structures of all compounds were characterized by Fourier-transform ınfrared spectroscopy, Nuclear magnetic resonance and elemental analysis. Crystal structures of compounds <b>1a</b>, <b>1c</b>, <b>1f</b>, <b>2c</b> and <b>2d</b> were investigated by single crystal X-ray crystallography. The compounds were evaluated for their DNA binding properties <i>via in vitro</i> spectrophotometric and <i>in silico</i> molecular docking studies. The compounds were found to interact with DNA <i>via</i> a groove binding mode with considerable the binding constants. The groove binding mode of interactions were also suggested by fluorescence ethidium bromide replacement experiments and viscosity studies. Binding interactions of the compounds with DNA have also been studied by molecular docking studies.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-14"},"PeriodicalIF":2.7,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143992673","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}