ArticleBioinformation2024
Screening of Leptin-LepR modulators using molecular docking and binding assay.
Article in Bioinformation, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 authors.
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Abstract
Leptin is a pleiotropic hormone which, upon binding to its cognate leptin receptor (LepR), induces the activation of the JAK2/ERK, STAT3/STAT5 and IRS/PI3 kinase signaling cascades. Hence, we used molecular docking and a chemical library to identify 18 compounds with high probability of interacting with the leptin binding domain (LBD) of LepR. 6 out of 18 compounds were selected based on toxicological and physicochemical properties to evaluate their effect in the formation of Leptin-LepR complex using ELISA assays. The six compounds showed discreet but significant modulation on the complex formation. These results have important implications in proposing novel strategies for modulating the formation of the Leptin-LepR complex, as therapeutic alternatives for patho-physiologies where the formation of this complex is deregulated.
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