Journal of Biomolecular Structure & Dynamics最新文献

{"title":"Exploring the Antarctic aminopeptidase P from <i>Pseudomonas</i> sp. strain AMS3 through structural analysis and molecular dynamics simulation.","authors":"Muhamad Nadzmi Omar, Raja Noor Zaliha Raja Abd Rahman, Noor Dina Muhd Noor, Wahhida Latip, Victor Feizal Knight, Mohd Shukuri Mohamad Ali","doi":"10.1080/07391102.2024.2331093","DOIUrl":"10.1080/07391102.2024.2331093","url":null,"abstract":"<p><p>Aminopeptidase P (APPro) is a crucial metalloaminopeptidase involved in amino acid cleavage from peptide N-termini, playing essential roles as versatile biocatalysts with applications ranging from pharmaceuticals to industrial processes. Despite acknowledging its potential for catalysis in lower temperatures, detailed molecular basis and biotechnological implications in cold environments are yet to be explored. Therefore, this research aims to investigate the molecular mechanisms underlying the cold-adapted characteristics of APPro from <i>Pseudomonas</i> sp. strain AMS3 (AMS3-APPro) through a detailed analysis of its structure and dynamics. In this study, structure analysis and molecular dynamics (MD) simulation of a predicted model of AMS3-APPro has been performed at different temperatures to assess structural flexibility and thermostability across a temperature range of 0-60 °C over 100 ns. The MD simulation results revealed that the structure were able to remain stable at low temperatures. Increased temperatures present a potential threat to the overall stability of AMS3-APPro by disrupting the intricate hydrogen bond networks crucial for maintaining structural integrity, thereby increasing the likelihood of protein unfolding. While the metal binding site at the catalytic core exhibits resilience at higher temperatures, highlighting its local structural integrity, the overall enzyme structure undergoes fluctuations and potential denaturation. This extensive structural instability surpasses the localized stability observed at the metal binding site. Consequently, these assessments offer in-depth understanding of the cold-adapted characteristics of AMS3-APPro, highlighting its capability to uphold its native conformation and stability in low-temperature environments. In summary, this research provides valuable insights into the cold-adapted features of AMS3-APPro, suggesting its efficient operation in low thermal conditions, particularly relevant for potential biotechnological applications in cold environments.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6239-6251"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140331736","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":"Revisiting <i>Plasmodium falciparum</i> P-type ATPase 4 in malarial: ADMET, mutation effect, and molecular simulation studies of potential inhibitors.","authors":"Iseoluwa Isaac Ajayi, Toluwase Hezekiah Fatoki, Ayodele Sunday Alonge, Courage Dele Famusiwa, Ibrahim Olabayode Saliu, Blessing Anuoluwapo Ejimadu, Mayowa Oluwalana Obafemi","doi":"10.1080/07391102.2025.2516757","DOIUrl":"10.1080/07391102.2025.2516757","url":null,"abstract":"<p><p>Malaria, a life-threatening disease caused by Plasmodium parasites, remains a major global health concern, with 247 million cases and approximately 627,000 deaths reported in 2020 across 84 malaria-endemic countries. The <i>Plasmodium falciparum</i> P-type ATPase 4 (PfATP4) gene is expressed throughout the parasite's asexual erythrocytic cycle and plays a vital role in regulating sodium ion levels in the plasma membrane. This study aimed to computationally evaluate selected clinical candidate compounds targeting PfATP4, focusing on their pharmacokinetics and molecular binding characteristics to support further drug development. Pharmacokinetic analyses revealed that Concanamycin A, Maduramicin, and GNF-Pf4492 exhibit low gastrointestinal absorption, while Brefeldin A, MMV396719, MMV006239, and Cipargamin can cross the blood-brain barrier. Among these, Brefeldin A and MMV006239 showed the lowest toxicity. Molecular docking revealed that (+)-SJ733 had the highest binding affinity (-8.891 kcal/mol), followed by MMV665878 (-7.796 kcal/mol) and Maduramicin (-7.791 kcal/mol). All 11 compounds showed binding affinities below -7.000 kcal/mol. Molecular dynamics simulations indicated stable interactions between PfATP4 and both (+)-SJ733 and MMV665878, involving key residues such as PHE917, GLN921, ARG985, and THR993. MMGBSA analysis showed that the MMV665878-PfATP4 complex was more stable and energetically favorable than the (+)-SJ733-PfATP4 complex under simulated physiological conditions. In conclusion, (+)-SJ733 and MMV665878 demonstrate strong potential as PfATP4 inhibitors, with different interaction profiles. Further <i>in vivo</i> and pharmacometric studies are required to validate their efficacy and determine optimal dosing strategies for malaria treatment.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6419-6434"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144289451","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":"Unveiling fructose and glucose binding to human serum albumin: fluorescence measurements and docking, molecular dynamics and quantum biochemistry computations.","authors":"André Hadad, Victor L B França, Marcos William Crisostomo, Kellen Brunaldi, Hernandes F Carvalho, Valder N Freire","doi":"10.1080/07391102.2024.2310211","DOIUrl":"10.1080/07391102.2024.2310211","url":null,"abstract":"<p><p>This research examines the interaction between human serum albumin (HSA) and various sugar forms (β-D-fructofuranose (FRC), α-D-glucopyranose (GLC), Keto-D-fructose (FRO), Aldehydo-D-glucose (GLO), and modified Aldehydo-D-glucose (GLOm)) using fluorescent spectroscopy, molecular docking simulations, molecular dynamics, protein conformational clusters (EnGens), molecular fractionation with conjugate caps (MFCC) and quantum biochemistry analysis. We analyze molecular and quantum aspects, uncovering interaction energies between sugar atoms and amino acids. Total interaction energy considers protein fragmentation, energetic decomposition, and interaction energy from a bottom-up perspective. Molecular dynamics reveal that unmodified Aldehydo-D-glucose (GLO) escapes HSA binding sites, explaining gradual glycation. We pioneer studying HSA's binding mechanism with glucose and fructose in a 1:1 ratio using long molecular dynamics simulations. Results suggest the transitional GLOm form has a higher Sudlow I site propensity than unmodified glucose, crucial for K195 glycation. FRO and GLOm interaction tendencies move toward a deeper FA7 cavity, near its center. This approach effectively elucidates small molecule binding mechanisms, consistent with previous experimental results.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6770-6790"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139575895","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":"CDH1 gene as biomarker towards breast cancer prediction.","authors":"Srijan Banerjee, Antara Sengupta, Shankar Kumar Ghosh, Raja Banerjee","doi":"10.1080/07391102.2024.2316770","DOIUrl":"10.1080/07391102.2024.2316770","url":null,"abstract":"<p><p>Breast cancer is considered to be happened due to genetic aberration. Out of several genes expressed, it is found that cadherin 1, type 1 (CDH1) is responsible in several ways to control the metabolic order in human. Deregulation of the function of protein E-cadherin, expressed from CDH1 plays an important role in lobular breast cancer. In order to understand the root cause of this recent claim, we focus on CDH1 gene: whether the genetic information translated due to any deviation/alteration/modification in its sequence is related to the occurrence of the different types breast cancer. Towards this end, quantitative analysis of different biophysical and bio-chemical properties of CDH1 gene in genomic and proteomic levels from the available genomic (cDNA) sequences of CDH1 gene (obtained from the COSMIC Database for 78 patients, suffering from various types of breast cancer) clearly emphasizes that alternation/modification in the sequence of the CDH1 gene can be detrimental. Furthermore, Random forest, K-nearest neighbour and stochastic gradient descent (SGD) algorithms are applied on the derived dataset to classify the types of breast cancer, and to validate our hypothesis regarding the acute role of CDH1 as potential bio marker for breast cancer. Analysis of the mutated CDH1 gene sequences, and their related parameters using aforesaid machine learning techniques clearly establish that CDH1 gene can take the deterministic role in predicting the chances of occurrences of different types of breast cancer with an accuracy of <math><mrow><mo>></mo><mn>90</mn><mi>%</mi></mrow><mo>.</mo></math> Such an observation opens a new paradigm in diagnostic approach of breast cancer.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6474-6487"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139905723","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":"Discovery of novel inhibitor via molecular dynamics simulations against D-alanyl-D-alanine carboxypeptidase of <i>Enterobacter cloacae</i>.","authors":"Faisal Ahmad, Saba Ismail, Syed Sikander Azam","doi":"10.1080/07391102.2024.2316790","DOIUrl":"10.1080/07391102.2024.2316790","url":null,"abstract":"<p><p>Antibiotics resistance by bacterial pathogens is a major concern to public health worldwide resulting in high health care costs and rising mortality. Subtractive proteomics prioritized D-alanyl-D-alanine carboxypeptidas (DacB) enzyme from Enterobacter cloacae ATCC 13047 as a potential candidate for drugs designing to block pathogen cell wall biosynthesis. Virtual screening of an antibacterial library against the target unraveled a hit compound (2-[(1-methylsulfonylpiperidin-3-yl)methyl]-6-(1H-pyrazol-4-yl) pyrazine) showing high affinity and stability with the target. The N-methyl-N-propyl-methanesulfonamide of the compound is seen as a closed affinity towards domain involving strong hydrogen bonds with Ser41, Lys44, Ser285, and Asn287. The 4-methyl-1H-pyrazole is posed towards the open cavity of domain I and II and formed hydrophobic and hydrophilic contacts. The system is highly stable with average carbon-alpha deviations of 1.69 Å over trajectories of 400-ns. Three vital residues projected: Arg437, Arg438 and Leu400 from enzyme pocket <i>via</i> Radial distribution function (RDF) assay, which actively engaged the inhibitor. Further confirmation is done by estimating binding free energies, which confirms the very low delta energy of -7.24 kcal/mol in Generalized Born (GB) method and -7.4363 kcal/mol in Poisson-Boltzmann (PB) method. WaterSwap calculations were performed that revealed the energies highly converged, an agreement on good system stability. Lastly, three DacB mutants were created to investigate the role of functional active residues and a decline in binding affinity of the residues was noticed. These computational results provide a gateway for experimentalists to further confirm their efficacy both in-vitro and in-vivo.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6816-6831"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139905724","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":"MMV method: a new approach to compare protein sequences under binary representation.","authors":"Jayanta Pal, Soumen Ghosh, Bansibadan Maji, Dilip Kumar Bhattacharya","doi":"10.1080/07391102.2024.2317982","DOIUrl":"10.1080/07391102.2024.2317982","url":null,"abstract":"<p><p>In the present work, a new form of descriptor using minimal moment vector (MMV) is introduced to compare protein sequences in the frequency domain under their component wise binary representations. From every sequence, 20 different binary component sequences are formed, each corresponding to 20 amino acids. Each such vector is now shifted from the time domain to the frequency domain by applying the Fast Fourier Transform (FFT). Next, the power spectrum calculated from the FFT values for each component sequence is so normalized that the sum of the components equals 1. The descriptor is defined as a 20-component vector composed of the 20 second-order minimal moments calculated from the normalized spectrum of the 20 component sequences. Once the descriptor is known, the distance matrix is created by applying the Euclidean Distance measure. The phylogenetic tree is generated by applying the unweighted pair group method with the arithmetic mean (UPGMA) algorithm using Molecular Evolutionary Genetics Analysis11 (MEGA11) software. In this work, the datasets used for similarity studies are 9 NADH dehydrogenase 5 (ND5), 12 Baculoviruses, 24 Transferrins (TF) proteins, and 50 Spike Protein of coronavirus. A qualitative measure using rationalized perception is used to compare the effectiveness of the proposed method. Quantitative measure based on symmetric distance (SD) is used to compare the phylogenetic trees of the present method with those obtained by other methods. It is observed that the phylogenetic trees generated by the proposed technique are at par with their known biological references, and they produce results better than those of the earlier methods.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6563-6569"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139905725","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 phytocompounds as potent inhibitors of sodium/glucose cotransporter-2 leading to diabetes treatment.","authors":"Ananta Swargiary, Manita Daimari, Arup Swargiary, Arup Biswas, Dulur Brahma, Hiloljyoti Singha","doi":"10.1080/07391102.2024.2319674","DOIUrl":"10.1080/07391102.2024.2319674","url":null,"abstract":"<p><p>Type-II diabetes, a major metabolic disorder has threatened the very existence of a healthy life since long ago. Commercially available antidiabetic drugs are known for several adverse effects. The present study attempted to identify potential phytocompounds as inhibitors of sodium/glucose cotransporter-2 (SGLT2), a major protein that helps in glucose re-absorption from renal tubules. A total of 28 phytocompounds were collected based on the literature survey. 3D co-ordinates of phytocompounds were collected from PubChem database. Molecular docking was carried out with SGLT2 protein and the best 3 docking complexes were subjected to molecular dynamics simulation for 100 ns. Free energy changes were also analyzed using MM/PBSA analysis. Phytocompounds were also analyzed for their drug-likeness and ADMET properties. Docking study observed a strong binding affinity of phytocompounds (> -7.0 kcal/mol). More than 10 phytocompounds showed better binding affinity compared to reference drugs. Further analysis of three best docking complexes when analyzed by MD simulation showed better stability and compactness of the complexes compared to reference drug, empagliflozin. MM/PBSA analysis also revealed that van der Waals force and electrostatic energy are the major binding energy involved in the complex formation. Like docking energy, free energy analysis also observed stronger binding energies (ΔGGAS) in SGLT2-phytocompound complexes compared to empagliflozin complex. All the phytocompounds showed drug-likeness and considerable ADMET properties. The study, therefore, suggests that Trifolirhizin-6'-monoacetate, Aspalathin, and Quercetin-3-glucoside could be a possible inhibitor of SGLT2 protein. However, further studies need to be carried out to reveal the exact mode of activity.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6667-6680"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139912697","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 the odorant binding proteins of Western Flower Thrips (<i>Frankliniella occidentalis</i>), characterization and binding analysis of <i>FoccOBP3</i> with molecular modelling, molecular dynamics simulations and a confirmatory field trial.","authors":"Zeeshan Zafar, Martyn J Wood, Sidra Fatima, Muhammad Faraz Bhatti, Farooq A Shah, Zack Saud, E Joel Loveridge, Ismail Karaca, Tariq M Butt","doi":"10.1080/07391102.2024.2317990","DOIUrl":"10.1080/07391102.2024.2317990","url":null,"abstract":"<p><p>Olfactory systems are indispensable for insects as they, including Western Flower Thrips (<i>Frankliniella occidentalis</i>), use olfactory cues for ovipositing and feeding. <i>F. occidentalis</i> use odorant binding proteins (OBPs) to transport semiochemicals to odorant receptors to induce a behavioural response from the sensillum lymph of the insect's antennae. This study identifies four OBPs of <i>F. occidentalis</i> and analyses their expression at three stages of growth: larvae, adult males and adult females. Further, it investigates the presence of conserved motifs and their phylogenetic relationship to other insect species. Moreover, <i>FoccOBP3</i> was <i>in silico</i> characterized to analyse its structure along with molecular docking and molecular dynamics simulations to understand its binding with semiochemicals of <i>F. occidentalis</i>. Molecular docking revealed the interactions of methyl isonicotinate, p-anisaldehyde and (S)-(-)-verbenone with <i>FoccOBP3</i>. Moreover, molecular dynamics simulations showed bonding stability of these ligands with <i>FoccOBP3,</i> and field trials validated that Lurem TR (commercial product) and p-anisaldehyde had greater attraction as compared to (S)-(-)-verbenone, given the compound's binding with <i>FoccOBP3</i>. The current study helps in understanding the tertiary structure and interaction of <i>FoccOBP3</i> with lures using computational and field data and will help in the identification of novel lures of insects in the future, given the importance of binding with OBPs.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"6853-6868"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139982965","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":"Attenuation of Type IV pili activity by natural products.","authors":"Kerem Yalkut, Soumaya Ben Ali Hassine, Esra Basaran, Ceyda Kula, Aslıhan Ozcan, Fatma Gizem Avci, Ozlem Keskin, Berna Sariyar Akbulut, Pemra Ozbek","doi":"10.1080/07391102.2024.2310781","DOIUrl":"10.1080/07391102.2024.2310781","url":null,"abstract":"<p><p>The virulence factor Type IV pili (T4P) are surface appendages used by the opportunistic pathogen <i>Pseudomonas aeruginosa</i> for twitching motility and adhesion in the environment and during infection. Additionally, the use of these appendages by <i>P. aeruginosa</i> for biofilm formation increases its virulence and drug resistance. Therefore, attenuation of the activity of T4P would be desirable to control <i>P. aeruginosa</i> infections. Here, a computational approach has been pursued to screen natural products that can be used for this purpose. PilB, the elongation ATPase of the T4P machinery in <i>P. aeruginosa</i>, has been selected as the target subunit and virtual screening of FDA-approved drugs has been conducted. Screening identified two natural compounds, ergoloid and irinotecan, as potential candidates for inhibiting this T4P-associated ATPase in <i>P. aeruginosa</i>. These candidate compounds underwent further rigorous evaluation through molecular dynamics (MD) simulations and then through <i>in vitro</i> twitching motility and biofilm inhibition assays. Notably, ergoloid emerged as a particularly promising candidate for weakening the T4P activity by inhibiting the elongation ATPases associated with T4P. This repurposing study paves the way for the timely discovery of antivirulence drugs as an alternative to classical antibiotic treatments to help combat infections caused by <i>P. aeruginosa</i> and related pathogens.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"5719-5729"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139671898","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":"Intelligent deep learning-based disease monitoring system in 5G network using multi-disease big data.","authors":"Anupam Das","doi":"10.1080/07391102.2024.2310785","DOIUrl":"10.1080/07391102.2024.2310785","url":null,"abstract":"<p><p>Recently, real-world disease monitoring techniques designed based on wearable medical equipment efficiently minimize the mortality rate. Initially, the data are manually collected from the patients to predict five diseases using 5 G frameworks. Then, the collected data are pre-processed to obtain high-quality data using the techniques like contrast enhancement, median filtering, fill empty space, remove repeated value and stemming. The pre-processed data are taken for extracting the features using a One-Dimensional Convolutional Neural Network (1D-CNN) to obtain the deep features. The parameters like hidden neuron count and epoch are tuned by the proposed Modified Predator Presence Probability-based Squirrel Search-Glowworm Swarm Optimization (MPPP-SSGSO) algorithm to enhance the variance. Then, the extracted features acquired using the 1D-CNN are given to the ensemble boosting-based models for predicting the score, which is combined by comprising approaches like Adaptive Boosting (AdaBoost), eXtreme Gradient Boosting (XGBoost) and Category Boosting (CatBoost). Further, the predicted scores obtained from such models are concatenated and passed to the Ensemble Boosting Scores-based Fuzzy Classifier (EBS-FC) for classifying the five different diseases. Here, the membership function of the fuzzy is optimized by the same developed MPPP-SSGSO algorithm for enhancing accuracy. Experiments are conducted, and validation is performed, which showcased that the recommended framework achieved a better outcome rate than the conventional techniques. Finally, the suggested strategy outperforms the current state-of-the-art methods with an accuracy rate of 91.34%.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"5730-5755"},"PeriodicalIF":2.4,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139706895","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}