ArticleJournal of computer-aided molecular design2026
Insights into the binding mechanism and structural requirements of LPAR2 antagonists as antifibrotic agents based on homology modeling, molecular docking, prediction of membrane permeability and 3D QSAR.
Article in Journal of computer-aided molecular design, 2026. 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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Abstract
Lysophosphatidic acid receptor 2 (LPAR2), a G protein-coupled receptor, has been implicated in the progression of fibrosis and is therefore a promising novel drug target for the treatment of fibrosis and related diseases. In this paper, a reliable homology model of LPAR2 was obtained by using three templates (PDB IDs: 4Z34, 7TD0, and 7VIE) and evaluations. A new binding site for a series of selective LPAR2 inhibitors were identified through molecular docking with the reference compound 50. Subsequently, a three-dimensional quantitative structure-activity relationship (3D QSAR) analysis was conducted on a series of N-sulfonyl heterocyclic antagonists of LPAR2. The derived optimal CoMFA model (q
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