{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T14:27:40Z","timestamp":1787840860726,"version":"build-2784847793"},"reference-count":80,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"4","license":[{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,7]]},"abstract":"<jats:sec>\n                    <jats:title>Background and purpose:<\/jats:title>\n                    <jats:p>\n                      Leishmaniasis has been categorized as one of the most significant tropical illnesses, often ignored. This study aimed to find effective plant compounds to combat the pathogenicity of the\n                      <jats:italic toggle=\"yes\">Leishmania<\/jats:italic>\n                      parasite.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Experimental approach:<\/jats:title>\n                    <jats:p>\n                      The 3D structures of the zinc leishmanolysin glycoprotein 63 (GP63), farnesyl diphosphate synthase (FPPS), and N-myristoyltransferase (NMT) proteins from\n                      <jats:italic toggle=\"yes\">L. major,<\/jats:italic>\n                      as well as blockers and 4000 herbal compounds, were retrieved from the PubChem database. A molecular docking study was performed on\n                      <jats:italic toggle=\"yes\">Leishmania<\/jats:italic>\n                      proteins using PyRx software. The activity, ADMET characteristics, and daily carcinogenicity were taken from \u201cSwiss ADME\u201d, \u201cway 2 drug\u201d, and \u201cLazar\u201d websites. Molecules with the greatest docking scores for each protein were chosen for molecular dynamics simulation using GROMACS.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Findings\/Results:<\/jats:title>\n                    <jats:p>Molecular docking experiments revealed that withaperuvin D and lagerstannin A have a strong affinity for the GP63 protein. Moreover, strictinin showed the highest binding affinity for FPPS, whereas the top compounds for NMT were chelidimerine, friedelin, and hypericin. Additionally, luteolin 3'-o-glucuronide, protohypericin, and amentoflavone had high binding affinity for all three proteins, and amentoflavone had the highest binding energy of all the proteins. Based on RMSD, RMSF, Rg, PCA, MM\/PBSA binding energy, and SASA, the molecular dynamic simulation results indicated relatively stable interactions between these ligands and the mentioned proteins during the simulation period.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion and implications:<\/jats:title>\n                    <jats:p>Given the pharmaceutical information, the mentioned substances may have anti-inflammatory and wound-healing properties in addition to blocking proteins. Therefore, experimentally examining these compounds in the future can help control and treat leishmaniasis.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/rps.rps_123_24","type":"journal-article","created":{"date-parts":[[2025,8,26]],"date-time":"2025-08-26T03:03:18Z","timestamp":1756177398000},"page":"535-565","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":1,"title":["Molecular docking and simulation analysis of selected herbal compounds against GP63, FPPS, and NMT, three important Leishmania major proteins"],"prefix":"10.4103","volume":"20","author":[{"given":"Seyed Mahmoud","family":"Mousavi","sequence":"first","affiliation":[{"name":"Department of Parasitology and Mycology, School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Negar","family":"Balmeh","sequence":"additional","affiliation":[{"name":"Department of Research 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