Journal of Biomolecular Structure & Dynamics最新文献

{"title":"In silico studies for improving target selectivity of anti-malarial dual falcipain inhibitors vis-à-vis human cathepsins.","authors":"Jeevan Patra, Smriti Arora, Utsab Debnath, Neeraj Mahindroo","doi":"10.1080/07391102.2024.2427372","DOIUrl":"https://doi.org/10.1080/07391102.2024.2427372","url":null,"abstract":"<p><p>Dual falcipain-2 (FP-2) and falcipain-3 (FP-3) inhibitors, <b>NM12</b> and <b>NM15</b>, displayed micromolar inhibitions but they exhibit similar binding affinities for the human cathepsins, thus indicating potential toxicity. The current study aims to develop a model to enhance the selectivity of the falcipain inhibitors vis-à-vis human cathepsins using previously identified dual falcipain 2 and 3 inhibitors, <b>NM12</b> and <b>NM15</b>. To improve the selectivity of <b>NM12</b> and <b>NM15</b>, analogs with weaker interactions with the conserved residues in the FPs and hCatK were designed while enhancing the unique interactions for the FPs. In silico analysis was carried out in the S2 subsite of both plasmodium and human proteases which is considered the preferred selective site due to the presence of less conserved residues. The Fasta sequence alignment and active/conserved binding site superimposition show that FPs contain acidic polar residues (Asp234 for FP2 and Glu243 for FP3) while hCatK has a neutral hydrophobic residue (Leu209) at the S2 subsite. Therefore, analogs of NM12 and NM15 were designed to enhance affinity and selectivity by improving interactions with these acidic residues while avoiding interactions with hydrophobic residues in hCatK. Newly designed analogs (<b>NM12H and NM15G</b>) show better selectivity as well as binding affinity towards FPs (<b>ΔG of NM12H</b>: -74.49 kcal/mol for FP2, -70.97 kcal/mol for FP3; <b>ΔG of NM15G:</b> -70.09 kcal/mol for FP2, -74.52 kcal/mol for FP3) as compared to NM12 and NM15. Thus, the selectivity and binding affinity against dual falcipains vis-à-vis human cathepsin were improved using molecular dynamic simulations.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-20"},"PeriodicalIF":2.7,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142648337","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":"Hydrophobic forces at play: insights into AmelOBP4 and brood volatile interactions in <i>Apis mellifera</i> hygienic behavior.","authors":"Ramkumar Haran, Chakkarai Sathyaseelan, Ettiappan Sumathi, Jayakanthan Mannu","doi":"10.1080/07391102.2024.2429019","DOIUrl":"https://doi.org/10.1080/07391102.2024.2429019","url":null,"abstract":"<p><p>Understanding the intricate processes underlying olfaction necessitates unraveling the complexities of odorant binding protein's interactions with volatile compounds triggering hygienic behavior in <i>Apis mellifera</i>, This study delves into the intricate processes of olfaction by focusing on the interactions between <i>Apis mellifera</i> Odorant Binding Protein 4 (AmelOBP4) and volatile compounds associated with hygienic behavior, employing a comprehensive computational approach. Molecular docking analyses reveal detailed binding interactions, emphasizing the significance of hydrophobic interactions and specific amino acid residues in stabilizing AmelOBP4-volatile complexes, notably with 2-nonacosanone (-8.4 kcal/mol) and hexacosyl acetate (-8.4 kcal/mol). Molecular dynamics simulations demonstrate sustained stability and principal component analysis affirms structural integrity through restricted global motions. Binding free energy calculations underscore robust interactions, with per-residue free energy decomposition identifying key amino acids contributing significantly to binding affinity. These findings illuminate the pivotal role of hydrophobic interactions and specific residues (Phe 60, Leu 83, Ile 116, Leu 126, and Leu 130) in modulating AmelOBP4-volatile interactions, providing foundational insights into volatile-based applications and potential olfactory response modulation, contributing to our understanding of olfactory processes.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-15"},"PeriodicalIF":2.7,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142648335","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":"Molecular origin of the differential stabilities of the protofilaments in different polymorphs: molecular dynamics simulation and deep learning.","authors":"Premananda Basak, Nibedita Ray Chaudhuri, Debadrita Basu, Debabani Ganguly, Shubhra Ghosh Dastidar","doi":"10.1080/07391102.2024.2427364","DOIUrl":"https://doi.org/10.1080/07391102.2024.2427364","url":null,"abstract":"<p><p>Fragments of α-synuclein, an intrinsically disordered protein, whose misfolding and aggregation are responsible for diseases like Parkinson's disease and others, can co-exist in different polymorphs like 'rod' and 'twister'. Their apparently stable structures have different degrees of tolerance to perturbations like point mutations. The molecular basis of this is investigated using molecular dynamics-based conformational sampling. A charge-swapping mutation, E46K, known to be a reason for the early onset of Parkinson's disease, has differential impact on two polymorphs, and its molecular reason has been probed by investigating the intra-fibril interaction network that is responsible for stabilizing the aggregates. Two different quaternary level arrangement of the peptides in two polymorphs, establishing two different types of interrelations between residues of the peptide monomers, form the basis of their differential stabilities; a Deep Neural Network (DNN)-based analysis has extracted different pairs of residues and their spatial proximities as features to distinguish the states of two polymorphs. It has revealed that difference in these molecular arrangements intrinsically assigns key roles to different sets of residues in two different forms, like a feedback loop from quaternary structure to sequence level; an important insight into the sequence-structure relationship in general. Such atomic level insights were substantiated with the proof of differences in the dynamic correlation between residue pairs, altered mobilities of the sidechains that affects packing and redistribution of the weightage of different principal modes of internal motions in different systems. The identification of key residues with altered significance in different polymorphs is likely to benefit the planned design of fibril breaking molecules.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-17"},"PeriodicalIF":2.7,"publicationDate":"2024-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142648339","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":"Two groups and three classes of the conserved structural organization of nucleophile and non-canonical ElbowFlankOxy networks in different superfamily proteins.","authors":"Konstantin Denessiouk, Alexander I Denesyuk, Mark S Johnson, Vladimir N Uversky","doi":"10.1080/07391102.2024.2429798","DOIUrl":"https://doi.org/10.1080/07391102.2024.2429798","url":null,"abstract":"<p><p>The nucleophile elbow is a well-known structural motif, which exists in proteins with catalytic triads and contains a catalytic nucleophile and the first node of an oxyanion hole. Here, we show that structural similarities of proteins with the nucleophile elbow extend beyond simple nucleophile elbow motifs. The motifs are incorporated into larger conserved structural organizations, the ElbowFlankOxy networks, incorporating motifs and flanking residues and networks of conserved interactions. A detailed structural analysis shows two major types of ElbowFlankOxy networks, depending on the formation of the oxyanion hole. Additionally, the ElbowFlankOxy networks show three classes: Class 1-2-3, 3-1-2, and 2-3-1, defined by the order in which the catalytic nucleophile and key interacting residues are located in the amino acid sequence, giving rise to six ElbowFlankOxy network variations. This makes it possible to properly position homologous non-catalytic, non-standard, and unusual catalytic triad active sites of proteins with the nucleophile elbow within the fold classification.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-16"},"PeriodicalIF":2.7,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142638838","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":"Noncovalent inhibitors of DprE1 for tuberculosis treatment: design, synthesis, characterization, <i>in vitro</i> and <i>in silico</i> studies of 4-oxo-1,4-dihydroquinazolinylpyrazine-2-carboxamides.","authors":"Shivakumar, P Dinesha, D Udayakumar","doi":"10.1080/07391102.2024.2427368","DOIUrl":"https://doi.org/10.1080/07391102.2024.2427368","url":null,"abstract":"<p><p>In this study, we present a novel series of 4-oxo-1,4-dihydroquinazolinylpyrazine-2-carboxamide derivatives, which exert their inhibitory effect on decaprenylphosphoryl-β-D-ribose 2'-epimerase (DprE1) <i>via</i> the establishment of non-covalent interactions with the pivotal Cys387 residue located within the enzyme's active site. These compounds underwent scrutiny for their efficacy in combatting the <i>Mycobacterium tuberculosis</i> H37Rv strain, and compounds T8 and T13 exhibited promising antitubercular activity, boasting a minimal inhibitory concentration (MIC) of 7.99 and 8.27 µM respectively. Additionally, three compounds, T2, T3 and T12, showcased substantial antibacterial activity whereas compounds T12 and T13 exhibited pronounced antifungal efficacy. Remarkably, all active compounds demonstrated negligible cytotoxicity, and none posed harm to normal cells. To attain a more profound comprehension of the attributes of these compounds, we conducted <i>in silico</i> investigations to evaluate their Absorption, Distribution, Metabolism and Excretion properties. Additionally, molecular docking analyses were executed to elucidate their interactions with the DprE1 enzyme. Finally, Density Functional Theory studies were leveraged to explore the electronic characteristics of these compounds, thereby providing insights into their potential utility in the realm of pharmaceuticals.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-15"},"PeriodicalIF":2.7,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142638825","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":"Unraveling the physiochemical characteristics and molecular insights of Zein protein through structural modeling and conformational dynamics: a synergistic approach between machine learning and molecular dynamics simulations.","authors":"Amit Kumar Srivastav, Jyoti Jaiswal, Umesh Kumar","doi":"10.1080/07391102.2024.2428825","DOIUrl":"10.1080/07391102.2024.2428825","url":null,"abstract":"<p><p>This research article presents a comprehensive investigation into the three-dimensional structure, physicochemical characteristics and conformational stability of the Zein protein. Machine learning (ML) based homology modeling approach, was employed to predict the 3D structure of Zein protein. Convolutional neural networks (CNNs) were utilized for refining the model, capturing complex spatial features and improving decoy refinement. The predicted 3D structure of Zein protein showed a high-confidence score, i.e. C-score of 0.96. Physiochemical characteristic was also analyzed to investigate its protonation and deprotonation behavior across a range of pH values. A comprehensive analysis of the titration curve and electrostatic charges was performed to uncover valuable molecular insights into the zein protein's charge distribution, electrostatic interactions and potential conformational changes. Molecular dynamics (MD) simulations were performed to analyze the zein structural behavior under different pH values (2.0, 4.5, 6.8, 10.0 and 12.5), ionic strengths (0 mM, 25 mM, 50 mM, 75 mM, 100 mM) and temperatures (300K, 350K, 375K). Our results demonstrated the influence of these factors on zein protein's stability and conformational dynamics. At extreme pH values of 2.0 and 12.5, the Zein protein exhibited increased structural deviations and potential unfolding, while intermediate pH values closer to the protein's isoelectric point (pI) demonstrated more compact and stable conformations. Analysis of root mean square deviation, radius of gyration, solvent accessible surface area and Ramachandran plot provided clear understandings of the protein's compactness and surface exposure, confirming the impact of pH, ionic strength and temperature on the protein's conformation.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-20"},"PeriodicalIF":2.7,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142621347","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":"Molecular modeling and cytotoxic activity studies of oxirane-2-carboxylate derivatives.","authors":"Muhammed Tilahun Muhammed, Mustafa Er, Senem Akkoc","doi":"10.1080/07391102.2024.2428826","DOIUrl":"10.1080/07391102.2024.2428826","url":null,"abstract":"<p><p>In this study, five 3-aryloxirane-2-carboxylate derivatives were prepared, and the antiproliferative activities of molecules were screened in lung and colon cancer cell lines. The results showed that molecules had antiproliferative activity on cancerous cells with IC₅₀ values under 100 µM. Furthermore, all of the molecules were found to have a much higher cytotoxic effect than cisplatin in colon cancer cells. The interactions of the relatively active compounds to the crucial enzyme in cancer cell proliferation, cyclin-dependent kinase 1 (CDK1), were investigated using molecular docking. The stability of the resulting CDK1-compound complexes procured from the docking was also assessed through molecular dynamics (MD) simulations. Then, the binding affinity of compounds <b>2-3a</b> and <b>2-3c</b> to the target enzyme was computed by MMPBSA. The molecular docking study demonstrated that the two most active compounds could bind to the enzyme. The binding potential of <b>2-3a</b> is anticipated to be higher as it had one more conventional hydrogen bond and a slightly lower binding energy than compound <b>2-3c</b>. The MD simulation study exhibited that the two compounds formed a stable complex with the enzyme. On the other hand, the MMPBSA energy computation implicated a slightly higher binding affinity for compound <b>2-3c</b> toward the enzyme. Furthermore, electrical and frontier molecular orbital analysis of all of the tested compounds was conducted by density functional theory (DFT) studies. Compound <b>2-3a</b> is anticipated to be the most chemically stable as it gave the highest energy gap value in the DFT analysis.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-12"},"PeriodicalIF":2.7,"publicationDate":"2024-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142621310","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>Aspergillus terreus</i> MTCC6324 recombinant alcohol oxidase (rAOx): enhanced <i>in-silico</i> insight into structure, function, and substrate sequestration mechanism.","authors":"Mrityunjay Nigam, Mitun Chakraborty","doi":"10.1080/07391102.2024.2424946","DOIUrl":"https://doi.org/10.1080/07391102.2024.2424946","url":null,"abstract":"<p><p>Alcohol oxidase (AOx) enzymes have gained significant attention for their potential in industrial applications due to their unique ability to catalyze irreversible oxidation of diverse alcohol substrates without external co-factors. This study revisits and enhances <i>in-silico</i> work on <i>Aspergillus terreus</i> MTCC6324 recombinant AOx (rAOx) enzyme, combining artificial intelligence (AlphaFold), molecular docking (AutoDock Vina) techniques and Molecular dynamics (MD) simulations (Desmond). Comprehensive sequence analysis revealed a high degree of conservation among 23 AOx amino acid sequences from various <i>Aspergillus</i> species highlights conserved regions, affirming its GXGXXG Rossmann fold motif. AlphaFold-predicted 3D structure of rAOx demonstrated improved stereo-chemical stability compared to I-TASSER predicted structure with 87.6% amino acid residues in most favourable region of Ramachandran plot compared to 79.5%, respectively. Molecular docking revealed the binding affinities of co-factors FAD and diverse alcohol substrates, with cinnamyl alcohol exhibiting robust interaction with rAOx holoenzyme. MD simulations further elucidate the stability and dynamics of rAOx-FAD-cinnamyl alcohol complex over 100 nanoseconds. The simulations showcase FAD's stable binding within the protein core and highlights transient substrate interactions, dissociating within the active site after 75 ns suggesting a substrate sequestration mechanism. The study unveils substrate sequestration mechanism wherein cinnamyl alcohol exhibits temporary binding, leading to quick detachment from active site, mimicking reported exponential kinetics. This study not only validates previous findings but also offers a comprehensive understanding of intricate dynamics governing rAOx enzymatic activity. The improved sequence-to-structure prediction and detailed molecular insights into substrate sequestration provide a valuable foundation for future experimental investigations and rational design of bio-catalytic processes.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-12"},"PeriodicalIF":2.7,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142621341","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":"Targeting transcriptional regulatory protein RfaH with natural compounds to develop novel therapies against <i>Klebsiella pneumoniae</i>.","authors":"Anam Ashraf, Arunabh Choudhary, Mohammad Ali Khan, Saba Noor, Afzal Hussain, Mohamed F Alajmi, Md Imtaiyaz Hassan","doi":"10.1080/07391102.2024.2427376","DOIUrl":"10.1080/07391102.2024.2427376","url":null,"abstract":"<p><p>The growing threat of antibiotic-resistant <i>K. pneumoniae</i> infections demands novel treatment strategies. This study focuses on the transcriptional regulatory protein RfaH, a protein crucial for the bacteria's virulence by promoting gene expression for its capsule, cell wall, and pilus. As <i>K. pneumoniae</i> becomes resistant to existing antibiotics, targeting RfaH with specific inhibitors offers a promising alternative. The diverse benefits of natural compounds, including efficacy against microbial diseases, modulation of inflammatory processes, and potential in cancer therapy, have led to their increasing use in medicine. Through natural compound screening, we aimed to identify potential RfaH inhibitors and understand their interactions with the active site pocket of RfaH. Disrupting interactions of specific residues in RfaH by ligand binding could offer a means to interfere with its function selectively. We found that Naringenin and Quercetin have a strong binding affinity for RfaH β'CH binding pocket and form stable complexes, as evident from the MD simulation studies. The binding affinity of Naringenin and Quercetin was further validated experimentally by fluorescence measurements. This knowledge can be used to design potent and selective RfaH inhibitors for a new therapeutic approach to combat <i>K. pneumoniae</i> infections and address the urgent need for effective treatments.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-13"},"PeriodicalIF":2.7,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142621345","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, biological evaluation, and molecular modeling studies of some quinazolin-4(3<i>H</i>)-one-benzenesulfonamide hybrids as potential α-glucosidase inhibitors.","authors":"Emre Kadir Ayan, Güneş Çoban, Zeynep Soyer","doi":"10.1080/07391102.2024.2427373","DOIUrl":"https://doi.org/10.1080/07391102.2024.2427373","url":null,"abstract":"<p><p>Diabetes mellitus is a chronic metabolic disorder characterized by hyperglycemia, posing serious health risks and becoming increasingly prevalent. Prolonged hyperglycemia can lead to complications such as nephropathy, neuropathy, retinopathy, cardiovascular damage, and blindness. Controlling hyperglycemia through α-glucosidase inhibitors, which slow down carbohydrate breakdown, is an effective treatment strategy. However, current inhibitors like acarbose, voglibose, and miglitol while used to manage type 2 diabetes, have significant side effects. Therefore, developing new α-glucosidase inhibitors that are more effective and have fewer side effects is crucial. In this study, a series of novel quinazolin-4(3<i>H</i>)-one-benzenesulfonamide hybrid compounds were designed, synthesized, and evaluated for <i>in vitro</i> α-glucosidase inhibitory activity. The compounds showed higher enzyme inhibition potency, with IC₅₀ values ranging between 129.2 ± 0.5 and 558.7 ± 13.7 µM, compared to acarbose (IC₅₀=814.3 ± 13.5 µM). Among the tested compounds, compound <b>10</b>, bearing a 4-chlorophenyl ring on the nitrogen atom of the sulfonamide group, was the most active, with an IC₅₀ value of 129.2 ± 0.5 µM. Enzyme kinetics analyses and molecular modeling studies were conducted to understand their inhibition mechanisms and interactions with the enzyme. The kinetic studies revealed a mixed-type inhibition model, indicating that the compounds bind to the enzyme-substrate complex with higher affinity than to the free enzyme. Molecular modeling results confirmed these findings. Additionally, <i>in silico</i> prediction studies showed that the selected compounds have favourable physicochemical and drug-like properties. These results suggest these compounds have potential for further optimization and development as effective α-glucosidase inhibitors for diabetes treatment.</p>","PeriodicalId":15272,"journal":{"name":"Journal of Biomolecular Structure & Dynamics","volume":" ","pages":"1-21"},"PeriodicalIF":2.7,"publicationDate":"2024-11-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142621277","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}