<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bryan John A. Magoling</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification of Potential COX-2 Inhibitors from Eleusine indica Through In Vitro Cyclooxygenase Assay, LC-MS/MS-based Profiling, Molecular Docking, and Molecular Dynamics Simulation</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anti-inflammation</style></keyword><keyword><style  face="normal" font="default" size="100%">COX2 inhibition</style></keyword><keyword><style  face="normal" font="default" size="100%">diosmetin</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug discovery</style></keyword><keyword><style  face="normal" font="default" size="100%">Eleusine indica</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular docking</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular dynamics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2026</style></year><pub-dates><date><style  face="normal" font="default" size="100%">July 2026</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">18</style></volume><pages><style face="normal" font="default" size="100%">1-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;Introduction: &lt;/strong&gt;Cyclooxygenase-2 (COX-2) is a key enzyme involved in the production of pro-inflammatory mediators and is an important target for anti-inflammatory drug development. This study investigated the anti-inflammatory potential of Eleusine indica through in vitro COX inhibition, LC–MS-based phytochemical profiling, and computational analyses to identify potential COX-2 inhibitory metabolites. &lt;strong&gt;Methods:&lt;/strong&gt; The methanolic leaf extract of E. indica was evaluated for COX-1 and COX-2 inhibitory activities. Metabolites were identified using liquid chromatography–mass spectrometry (LC–MS) and screened for drug-likeness, ADMET, and toxicity properties using SwissADME and ProTox-3.0. Selected metabolites were subjected to molecular docking against COX-2 (PDB ID: 4COX), and the top-ranked compound was further evaluated through a 100 ns molecular dynamics simulation. &lt;strong&gt;Results:&lt;/strong&gt; The extract exhibited significantly greater inhibition of COX-2 (IC50 = 4.0 μg/mL) than COX-1 (IC&lt;sub&gt;50&lt;/sub&gt; = 12.5 μg/mL; p = 0.0005), indicating preferential COX-2 inhibition. LC–MS analysis tentatively identified ten metabolites, among which diosmetin, sinapine, and senkyunolide I showed favorable drug-likeness, pharmacokinetic, and toxicity profiles. Molecular docking revealed that diosmetin exhibited the strongest binding affinity toward COX-2 (−7.8 kcal/mol), followed by senkyunolide I (−6.6 kcal/mol) and sinapine (−6.3 kcal/mol). Molecular dynamics simulations confirmed the stability of the diosmetin–COX-2 complex through reduced structural fluctuations, maintained protein compactness, and persistent hydrogen-bond interactions. &lt;strong&gt;Conclusions: &lt;/strong&gt;Diosmetin emerged as the most promising metabolite from E. indica, exhibiting favorable pharmacokinetic, safety, docking, and molecular dynamics profiles. These findings suggest that diosmetin is a promising natural COX-2 inhibitor that warrants further experimental validation.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Original Article</style></work-type><section><style face="normal" font="default" size="100%">1</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;Bryan John A. Magoling&lt;sup&gt;1,2*&lt;/sup&gt; &lt;/strong&gt;&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;1&lt;/sup&gt;Department of Chemistry, College of Arts and Sciences, Batangas State University, The National Engineering University Pablo Borbon, Rizal Avenue Extension, Batangas City 4200, PHILIPPINES&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;2&lt;/sup&gt;Material Testing and Calibration Center, STEER Hub, Batangas State University, The National Engineering University Alangilan, Alangilan, Batangas City 4200, PHILIPPINES&lt;/p&gt;
</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Yuditya Artha</style></author><author><style face="normal" font="default" size="100%">Arif Arrahman</style></author><author><style face="normal" font="default" size="100%">Azminah</style></author><author><style face="normal" font="default" size="100%">Arry Yanuar</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular Dynamic Simulation of Hydroxymethylglutaryl-CoA Reductase Inhibitors from Gnetum gnemon L. Seed Extract</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Gnetum gnemon L</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydroxymethylglutaryl-CoA reductase inhibitor</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular dynamics</style></keyword><keyword><style  face="normal" font="default" size="100%">Trans-resveratrol</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">June 2018</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://fulltxt.org/article/672</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">793-797</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Objective:&lt;/strong&gt; &lt;em&gt;Gnetum gnemon&lt;/em&gt; L. (melinjo) seed extract contained trans-resveratrol which has been shown to inhibit hydroxymethylglutaryl-CoA (HMG-CoA) reductase. Therefore it has a potent activity for lowering blood cholesterol. This study was carried out to determine the molecular dynamics simulation of HMG-CoA reductase inhibitors from &lt;em&gt;Gnetum gnemon&lt;/em&gt; L. seed extract. &lt;strong&gt;Methods:&lt;/strong&gt; Molecular dynamics simulation using AMBER was used. The simulation was set at 300 K as default temperature and 310 K, average human body temperature. The main parameters of this study were ligand-residue interaction, binding affinity, root mean square deviation (RMSD), root mean square fluctuation (RMSF), hydrogen bonds analysis, molecular mechanics Poisson Boltzmann surface area (MMPBSA), and molecular mechanics generalized born surface area (MMGBSA). &lt;strong&gt;Results:&lt;/strong&gt; In the simulation study, trans-resveratrol, trans-piceid, gnemonol M, gnemonoside B, viniferin and gnetin C had shown lower energy than HMG (PDB ID: MAH), the substrate of HMG-CoA Reductase. Free energy binding obtained from simulation was between 11.1 to -31.38 kcal/mol. &lt;strong&gt;Conclusion:&lt;/strong&gt; The simulation at 310 K was preferable than 300 K as more interactions were performed and higher affinity was obtained.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Original Article</style></work-type><section><style face="normal" font="default" size="100%">793</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Yuditya Artha, Arif Arrahman, Azminah, Arry Yanuar* &lt;/strong&gt;&lt;/p&gt;
&lt;p style=&quot;text-align: justify;&quot;&gt;Faculty of Pharmacy, Universitas Indonesia, Depok 16424 West Java, INDONESIA.&lt;/p&gt;</style></auth-address></record></records></xml>