| Literature DB >> 30831530 |
Wonbeen Choi1, Valente Villegas1, Hannah Istre2, Ben Heppler2, Niki Gonzalez2, Nicole Brusman2, Lindsey Snider2, Emily Hogle2, Janelle Tucker2, Alma Oñate2, Sandra Oñate2, Lili Ma2, Stefan Paula3.
Abstract
Inhibitors of the enzyme xanthine oxidase (XO) with radical scavenging properties hold promise as novel agents against reperfusion injuries after ischemic events. By suppressing the formation of damaging reactive oxygen species (ROS) by XO or scavenging ROS from other sources, these compounds may prevent a buildup of ROS in the aftermath of a heart attack or stroke. To combine these two properties in a single molecule, we synthesized and characterized the non-purine XO inhibitor caffeic acid phenethylester (CAPE) and 19 derivatives using a convenient microwave-assisted Knoevenagel condensation protocol. Varying systematically the number and positions of the hydroxyl groups at the two phenyl rings, we derived structure-activity relationships based on experimentally determined XO inhibition data. Molecular docking suggested that critical enzyme/inhibitor interactions involved π-π interactions between the phenolic inhibitor ring and Tyr914, hydrogen bonds between inhibitor hydroxyl groups and Glu802, and hydrophobic interactions between the CAPE phenyl ring and non-polar residues located at the entrance of the binding site. To effectively scavenge the stable radical DPPH, two hydroxyl groups in 1,2- or 1,4-position at the phenyl ring were required. Among all compounds tested, E-phenyl 3-(3,4-dihydroxyphenyl)acrylate, a CAPE analog without the ethyl tether, showed the most promising properties.Entities:
Keywords: Caffeic acid derivatives; Dual properties; Enzyme inhibition; Knoevenagel condensation; Ligand docking; Radical scavenging
Year: 2019 PMID: 30831530 DOI: 10.1016/j.bioorg.2019.02.049
Source DB: PubMed Journal: Bioorg Chem ISSN: 0045-2068 Impact factor: 5.275