ArticleJournal of molecular modeling2012
Exploration of the binding of curcumin analogues to human P450 2C9 based on docking and molecular dynamics simulation.
Article in Journal of molecular modeling, 2012. 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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0 citing papers in PubMed, 7 citations in OpenAlex.
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4 authors at 1 institution in 1 country.
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Abstract
Molecular docking and molecular dynamics (MD) simulations are used to investigate the interactions of curcumin analogues (CAs) with human cytochrome P450 2 C9 (CYP2C9 or 2 C9) and the conformations of their binding sites. In order to examine conformations of CAs/2 C9 and interaction characteristics of their binding sites, RMSDs, RMSFs, and B-factors are computed, and electrostatic and hydrophobic interactions between CAs and 2 C9 are analyzed and discussed. Results demonstrate that the most CAs studied lie 4~15 Å above the heme of CYP2C9. The presence of CAs makes some residues in bound CYP2C9s become more flexible. In the binding sites of A0/2 C9 and C0/2 C9, the formation of H-bond networks (or CA-water-residue bridges) enhances the interactions between CAs and 2 C9. The stronger inhibitory effects of A0, B0, and C0 on 2 C9 can be ascribed to stronger electrostatic and hydrophobic interactions in the binding sites of CAs/2 C9.
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