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Comparing the Interactions of Trichomonas vaginalis/gallinae Legumain-Like Cysteine Protease 1 (LEGU-1) and Human Legumain (LGMN) Protein Sequences with Proton Pump Inhibitor Drugs (Lansoprazole, Omeprazole, and Esomeprazole) by Bioinformatics Analyses

dc.contributor.authorKoseoglu, Ahmet Efe
dc.contributor.authorKutnu, Meltem
dc.contributor.authorOzgultekin, Buminhan
dc.contributor.authorKoseoglu, Gulsum Deniz
dc.contributor.authorNeziri, Sabina
dc.contributor.authorGoc, Bilge Irem
dc.contributor.authorSeflekci, Yusuf
dc.contributor.authorOzgenturk, Nehir Ozdemir
dc.contributor.authorMerdan, Yagmur Ekenoglu
dc.date.accessioned2026-06-27T15:26:19Z
dc.date.issued2025
dc.description.abstractPurposeThe flagellar parasite Trichomonas vaginalis is the main cause of trichomoniasis cases globally and is associated with a broad range of complications. Due to the diverse range of virulence factors participating in the attachment, proliferation and resistance of this pathogen, preventive and well-tolerated compounds are necessary. One of the virulence factors in T. vaginalis, the legumain-like cysteine protease LEGU-1 is of particular interest as a target due to its potential influence on trichomoniasis and tumor development in urogenital systems, as well as its closely related to the avian strain T. gallinae. Previous studies on antineoplastic proton pump inhibitors revealed they also have legumain (LGMN) inhibitory activities.MethodsTherefore, this study aimed to compare the molecular interactions of T. vaginalis/gallinae LEGU-1 and H. sapiens LGMN with proton pump inhibitor drugs (lansoprazole, omeprazole, and esomeprazole) through sequence analysis, 3D modeling, and molecular docking.ResultsAlthough sequence analyses revealed low homology between T. vaginalis/gallinae LEGU-1 and H. sapiens LGMN, secondary and 3D structural comparisons uncovered their structural conservation. Possible binding sites in all three proteins identified via CB-DOCK2 were compared to the previously described sites for LGMN, followed by targeted docking using Autodock Vina. Identification of amino acids mutually interacting with all three ligands by both programs revealed the overall conservation of the binding pockets. The variations in the number of amino acids within the binding sites for all three proteins displayed the variations in the binding energies for each ligand. Lansoprazole, omeprazole and esomeprazole were shown to bind T. vaginalis/gallinae LEGU-1 and H. sapiens LGMN, with lansoprazole having the highest binding energy.ConclusionConclusion Beyond our promising bioinformatics results, this study can guide further research on the development of alternative therapeutic methods against trichomoniasis and concomitant conditions.en
dc.description.urihttps://doi.org/10.1007/s11686-025-01187-9
dc.identifier.doi10.1007/s11686-025-01187-9
dc.identifier.eissn1896-1851
dc.identifier.issn1230-2821
dc.identifier.issue1
dc.identifier.pubmed41410717
dc.identifier.urihttps://hdl.handle.net/20.500.14981/70991
dc.identifier.volume71
dc.identifier.wos001643367100004
dc.language.isoeng
dc.publisherSPRINGER INT PUBL AG
dc.relation.ispartofACTA PARASITOLOGICA
dc.subjectTrichomonas
dc.subjectHuman
dc.subjectLEGU-1
dc.subjectLGMN
dc.subjectProton pump inhibitors
dc.subjectBioinformatics
dc.subjectIDENTIFICATION
dc.subjectParasitology
dc.subjectVeterinary Sciences
dc.subjectZoology
dc.titleComparing the Interactions of Trichomonas vaginalis/gallinae Legumain-Like Cysteine Protease 1 (LEGU-1) and Human Legumain (LGMN) Protein Sequences with Proton Pump Inhibitor Drugs (Lansoprazole, Omeprazole, and Esomeprazole) by Bioinformatics Analyses
dc.typeArticle
dspace.entity.typePublication
local.import.sourceWOS

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